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The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries
The histidine–aspartate (HD)-domain protein superfamily contains metalloproteins that share common structural features but catalyze vastly different reactions ranging from oxygenation to hydrolysis. This chemical diversion is afforded by (i) their ability to coordinate most biologically relevant tra...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8177086/ https://www.ncbi.nlm.nih.gov/pubmed/34094591 http://dx.doi.org/10.3390/catal10101191 |
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author | Langton, Michelle Sun, Sining Ueda, Chie Markey, Max Chen, Jiahua Paddy, Isaac Jiang, Paul Chin, Natalie Milne, Amy Pandelia, Maria-Eirini |
author_facet | Langton, Michelle Sun, Sining Ueda, Chie Markey, Max Chen, Jiahua Paddy, Isaac Jiang, Paul Chin, Natalie Milne, Amy Pandelia, Maria-Eirini |
author_sort | Langton, Michelle |
collection | PubMed |
description | The histidine–aspartate (HD)-domain protein superfamily contains metalloproteins that share common structural features but catalyze vastly different reactions ranging from oxygenation to hydrolysis. This chemical diversion is afforded by (i) their ability to coordinate most biologically relevant transition metals in mono-, di-, and trinuclear configurations, (ii) sequence insertions or the addition of supernumerary ligands to their active sites, (iii) auxiliary substrate specificity residues vicinal to the catalytic site, (iv) additional protein domains that allosterically regulate their activities or have catalytic and sensory roles, and (v) their ability to work with protein partners. More than 500 structures of HD-domain proteins are available to date that lay out unique structural features which may be indicative of function. In this respect, we describe the three known classes of HD-domain proteins (hydrolases, oxygenases, and lyases) and identify their apparent traits with the aim to portray differences in the molecular details responsible for their functional divergence and reconcile existing notions that will help assign functions to yet-to-be characterized proteins. The present review collects data that exemplify how nature tinkers with the HD-domain scaffold to afford different chemistries and provides insight into the factors that can selectively modulate catalysis. |
format | Online Article Text |
id | pubmed-8177086 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
record_format | MEDLINE/PubMed |
spelling | pubmed-81770862021-06-04 The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries Langton, Michelle Sun, Sining Ueda, Chie Markey, Max Chen, Jiahua Paddy, Isaac Jiang, Paul Chin, Natalie Milne, Amy Pandelia, Maria-Eirini Catalysts Article The histidine–aspartate (HD)-domain protein superfamily contains metalloproteins that share common structural features but catalyze vastly different reactions ranging from oxygenation to hydrolysis. This chemical diversion is afforded by (i) their ability to coordinate most biologically relevant transition metals in mono-, di-, and trinuclear configurations, (ii) sequence insertions or the addition of supernumerary ligands to their active sites, (iii) auxiliary substrate specificity residues vicinal to the catalytic site, (iv) additional protein domains that allosterically regulate their activities or have catalytic and sensory roles, and (v) their ability to work with protein partners. More than 500 structures of HD-domain proteins are available to date that lay out unique structural features which may be indicative of function. In this respect, we describe the three known classes of HD-domain proteins (hydrolases, oxygenases, and lyases) and identify their apparent traits with the aim to portray differences in the molecular details responsible for their functional divergence and reconcile existing notions that will help assign functions to yet-to-be characterized proteins. The present review collects data that exemplify how nature tinkers with the HD-domain scaffold to afford different chemistries and provides insight into the factors that can selectively modulate catalysis. 2020-10-15 2020-10 /pmc/articles/PMC8177086/ /pubmed/34094591 http://dx.doi.org/10.3390/catal10101191 Text en https://creativecommons.org/licenses/by/4.0/This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ). |
spellingShingle | Article Langton, Michelle Sun, Sining Ueda, Chie Markey, Max Chen, Jiahua Paddy, Isaac Jiang, Paul Chin, Natalie Milne, Amy Pandelia, Maria-Eirini The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries |
title | The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries |
title_full | The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries |
title_fullStr | The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries |
title_full_unstemmed | The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries |
title_short | The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries |
title_sort | hd-domain metalloprotein superfamily: an apparent common protein scaffold with diverse chemistries |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8177086/ https://www.ncbi.nlm.nih.gov/pubmed/34094591 http://dx.doi.org/10.3390/catal10101191 |
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