Cargando…
Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site
The substrate-binding protein YfeA (also known as YPO2439 or y1897) is a polyspecific metal-binding protein that is crucial for nutrient acquisition and virulence in Yersinia pestis, the causative microbe of plague. YfeA folds into a monomeric c-clamp like other substrate-binding proteins and has tw...
Autores principales: | , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8411934/ https://www.ncbi.nlm.nih.gov/pubmed/34473105 http://dx.doi.org/10.1107/S2053230X21008086 |
_version_ | 1783747369433563136 |
---|---|
author | Radka, Christopher D. Aller, Stephen G. |
author_facet | Radka, Christopher D. Aller, Stephen G. |
author_sort | Radka, Christopher D. |
collection | PubMed |
description | The substrate-binding protein YfeA (also known as YPO2439 or y1897) is a polyspecific metal-binding protein that is crucial for nutrient acquisition and virulence in Yersinia pestis, the causative microbe of plague. YfeA folds into a monomeric c-clamp like other substrate-binding proteins and has two metal-binding sites (sites 1 and 2). Site 2 is a bidentate surface site capable of binding Zn and Mn atoms and is a unique feature of YfeA. Occasionally, the site 2 residues of two YfeA molecules will cooperate with the histidine tag of a third YfeA molecule in coordinating the same metal and lead to metal-dependent crystallographic packing. Here, three crystal structures of YfeA are presented at 1.85, 2.05 and 2.25 Å resolution. A comparison of the structures reveals that the metal can be displaced at five different locations ranging from ∼4 to ∼16 Å away from the canonical site 2. These observations reveal different configurations of site 2 that enable cooperative metal binding and demonstrate how site 2 is dynamic and freely available for inter-protein metal coordination. |
format | Online Article Text |
id | pubmed-8411934 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-84119342021-09-13 Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site Radka, Christopher D. Aller, Stephen G. Acta Crystallogr F Struct Biol Commun Research Communications The substrate-binding protein YfeA (also known as YPO2439 or y1897) is a polyspecific metal-binding protein that is crucial for nutrient acquisition and virulence in Yersinia pestis, the causative microbe of plague. YfeA folds into a monomeric c-clamp like other substrate-binding proteins and has two metal-binding sites (sites 1 and 2). Site 2 is a bidentate surface site capable of binding Zn and Mn atoms and is a unique feature of YfeA. Occasionally, the site 2 residues of two YfeA molecules will cooperate with the histidine tag of a third YfeA molecule in coordinating the same metal and lead to metal-dependent crystallographic packing. Here, three crystal structures of YfeA are presented at 1.85, 2.05 and 2.25 Å resolution. A comparison of the structures reveals that the metal can be displaced at five different locations ranging from ∼4 to ∼16 Å away from the canonical site 2. These observations reveal different configurations of site 2 that enable cooperative metal binding and demonstrate how site 2 is dynamic and freely available for inter-protein metal coordination. International Union of Crystallography 2021-08-24 /pmc/articles/PMC8411934/ /pubmed/34473105 http://dx.doi.org/10.1107/S2053230X21008086 Text en © Radka and Aller 2021 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Research Communications Radka, Christopher D. Aller, Stephen G. Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site |
title | Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site |
title_full | Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site |
title_fullStr | Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site |
title_full_unstemmed | Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site |
title_short | Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site |
title_sort | site 2 of the yersinia pestis substrate-binding protein yfea is a dynamic surface metal-binding site |
topic | Research Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8411934/ https://www.ncbi.nlm.nih.gov/pubmed/34473105 http://dx.doi.org/10.1107/S2053230X21008086 |
work_keys_str_mv | AT radkachristopherd site2oftheyersiniapestissubstratebindingproteinyfeaisadynamicsurfacemetalbindingsite AT allerstepheng site2oftheyersiniapestissubstratebindingproteinyfeaisadynamicsurfacemetalbindingsite |