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Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism
The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1 Å by single-wavelength anomalous dispersion and multiple-wavelength anomalous dispersion, respectively, using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as p...
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
International Union of Crystallography
2010
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954203/ https://www.ncbi.nlm.nih.gov/pubmed/20944209 http://dx.doi.org/10.1107/S1744309109050647 |
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| author | Bakolitsa, Constantina Kumar, Abhinav Jin, Kevin K. McMullan, Daniel Krishna, S. Sri Miller, Mitchell D. Abdubek, Polat Acosta, Claire Astakhova, Tamara Axelrod, Herbert L. Burra, Prasad Carlton, Dennis Chen, Connie Chiu, Hsiu-Ju Clayton, Thomas Das, Debanu Deller, Marc C. Duan, Lian Elias, Ylva Ellrott, Kyle Ernst, Dustin Farr, Carol L. Feuerhelm, Julie Grant, Joanna C. Grzechnik, Anna Grzechnik, Slawomir K. Han, Gye Won Jaroszewski, Lukasz Johnson, Hope A. Klock, Heath E. Knuth, Mark W. Kozbial, Piotr Marciano, David Morse, Andrew T. Murphy, Kevin D. Nigoghossian, Edward Nopakun, Amanda Okach, Linda Paulsen, Jessica Puckett, Christina Reyes, Ron Rife, Christopher L. Sefcovic, Natasha Tien, Henry J. Trame, Christine B. Trout, Christina V. van den Bedem, Henry Weekes, Dana White, Aprilfawn Xu, Qingping Hodgson, Keith O. Wooley, John Elsliger, Marc-Andre Deacon, Ashley M. Godzik, Adam Lesley, Scott A. Wilson, Ian A. |
| author_facet | Bakolitsa, Constantina Kumar, Abhinav Jin, Kevin K. McMullan, Daniel Krishna, S. Sri Miller, Mitchell D. Abdubek, Polat Acosta, Claire Astakhova, Tamara Axelrod, Herbert L. Burra, Prasad Carlton, Dennis Chen, Connie Chiu, Hsiu-Ju Clayton, Thomas Das, Debanu Deller, Marc C. Duan, Lian Elias, Ylva Ellrott, Kyle Ernst, Dustin Farr, Carol L. Feuerhelm, Julie Grant, Joanna C. Grzechnik, Anna Grzechnik, Slawomir K. Han, Gye Won Jaroszewski, Lukasz Johnson, Hope A. Klock, Heath E. Knuth, Mark W. Kozbial, Piotr Marciano, David Morse, Andrew T. Murphy, Kevin D. Nigoghossian, Edward Nopakun, Amanda Okach, Linda Paulsen, Jessica Puckett, Christina Reyes, Ron Rife, Christopher L. Sefcovic, Natasha Tien, Henry J. Trame, Christine B. Trout, Christina V. van den Bedem, Henry Weekes, Dana White, Aprilfawn Xu, Qingping Hodgson, Keith O. Wooley, John Elsliger, Marc-Andre Deacon, Ashley M. Godzik, Adam Lesley, Scott A. Wilson, Ian A. |
| author_sort | Bakolitsa, Constantina |
| collection | PubMed |
| description | The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1 Å by single-wavelength anomalous dispersion and multiple-wavelength anomalous dispersion, respectively, using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). These proteins are the first structural representatives of the PF06684 (DUF1185) Pfam family. Structural analysis revealed that both structures adopt a variant of the Bacillus chorismate mutase fold (BCM). The biological unit of both proteins is a hexamer and analysis of homologs indicates that the oligomer interface residues are highly conserved. The conformation of the critical regions for oligomerization appears to be dependent on pH or salt concentration, suggesting that this protein might be subject to environmental regulation. Structural similarities to BCM and genome-context analysis suggest a function in amino-acid synthesis. |
| format | Text |
| id | pubmed-2954203 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 2010 |
| publisher | International Union of Crystallography |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-29542032010-10-27 Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism Bakolitsa, Constantina Kumar, Abhinav Jin, Kevin K. McMullan, Daniel Krishna, S. Sri Miller, Mitchell D. Abdubek, Polat Acosta, Claire Astakhova, Tamara Axelrod, Herbert L. Burra, Prasad Carlton, Dennis Chen, Connie Chiu, Hsiu-Ju Clayton, Thomas Das, Debanu Deller, Marc C. Duan, Lian Elias, Ylva Ellrott, Kyle Ernst, Dustin Farr, Carol L. Feuerhelm, Julie Grant, Joanna C. Grzechnik, Anna Grzechnik, Slawomir K. Han, Gye Won Jaroszewski, Lukasz Johnson, Hope A. Klock, Heath E. Knuth, Mark W. Kozbial, Piotr Marciano, David Morse, Andrew T. Murphy, Kevin D. Nigoghossian, Edward Nopakun, Amanda Okach, Linda Paulsen, Jessica Puckett, Christina Reyes, Ron Rife, Christopher L. Sefcovic, Natasha Tien, Henry J. Trame, Christine B. Trout, Christina V. van den Bedem, Henry Weekes, Dana White, Aprilfawn Xu, Qingping Hodgson, Keith O. Wooley, John Elsliger, Marc-Andre Deacon, Ashley M. Godzik, Adam Lesley, Scott A. Wilson, Ian A. Acta Crystallogr Sect F Struct Biol Cryst Commun Domains of Unknown Function The crystal structures of BB2672 and SPO0826 were determined to resolutions of 1.7 and 2.1 Å by single-wavelength anomalous dispersion and multiple-wavelength anomalous dispersion, respectively, using the semi-automated high-throughput pipeline of the Joint Center for Structural Genomics (JCSG) as part of the NIGMS Protein Structure Initiative (PSI). These proteins are the first structural representatives of the PF06684 (DUF1185) Pfam family. Structural analysis revealed that both structures adopt a variant of the Bacillus chorismate mutase fold (BCM). The biological unit of both proteins is a hexamer and analysis of homologs indicates that the oligomer interface residues are highly conserved. The conformation of the critical regions for oligomerization appears to be dependent on pH or salt concentration, suggesting that this protein might be subject to environmental regulation. Structural similarities to BCM and genome-context analysis suggest a function in amino-acid synthesis. International Union of Crystallography 2010-03-05 /pmc/articles/PMC2954203/ /pubmed/20944209 http://dx.doi.org/10.1107/S1744309109050647 Text en © Bakolitsa et al. 2010 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
| spellingShingle | Domains of Unknown Function Bakolitsa, Constantina Kumar, Abhinav Jin, Kevin K. McMullan, Daniel Krishna, S. Sri Miller, Mitchell D. Abdubek, Polat Acosta, Claire Astakhova, Tamara Axelrod, Herbert L. Burra, Prasad Carlton, Dennis Chen, Connie Chiu, Hsiu-Ju Clayton, Thomas Das, Debanu Deller, Marc C. Duan, Lian Elias, Ylva Ellrott, Kyle Ernst, Dustin Farr, Carol L. Feuerhelm, Julie Grant, Joanna C. Grzechnik, Anna Grzechnik, Slawomir K. Han, Gye Won Jaroszewski, Lukasz Johnson, Hope A. Klock, Heath E. Knuth, Mark W. Kozbial, Piotr Marciano, David Morse, Andrew T. Murphy, Kevin D. Nigoghossian, Edward Nopakun, Amanda Okach, Linda Paulsen, Jessica Puckett, Christina Reyes, Ron Rife, Christopher L. Sefcovic, Natasha Tien, Henry J. Trame, Christine B. Trout, Christina V. van den Bedem, Henry Weekes, Dana White, Aprilfawn Xu, Qingping Hodgson, Keith O. Wooley, John Elsliger, Marc-Andre Deacon, Ashley M. Godzik, Adam Lesley, Scott A. Wilson, Ian A. Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism |
| title | Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism |
| title_full | Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism |
| title_fullStr | Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism |
| title_full_unstemmed | Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism |
| title_short | Structures of the first representatives of Pfam family PF06684 (DUF1185) reveal a novel variant of the Bacillus chorismate mutase fold and suggest a role in amino-acid metabolism |
| title_sort | structures of the first representatives of pfam family pf06684 (duf1185) reveal a novel variant of the bacillus chorismate mutase fold and suggest a role in amino-acid metabolism |
| topic | Domains of Unknown Function |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954203/ https://www.ncbi.nlm.nih.gov/pubmed/20944209 http://dx.doi.org/10.1107/S1744309109050647 |
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