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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\u2005\u00c5 resolution. A comparison of the structures reveals that the metal can be displaced at five different locations ranging from \u223c4 to \u223c16\u2005\u00c5 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.<\/jats:p>","DOI":"10.1107\/s2053230x21008086","type":"journal-article","created":{"date-parts":[[2021,8,24]],"date-time":"2021-08-24T13:25:38Z","timestamp":1629811538000},"page":"286-293","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":3,"title":["Site 2 of the <i>Yersinia pestis<\/i> substrate-binding protein YfeA is a dynamic surface metal-binding site"],"prefix":"10.1107","volume":"77","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6037-7710","authenticated-orcid":true,"given":"Christopher D.","family":"Radka","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0379-5534","authenticated-orcid":true,"given":"Stephen G.","family":"Aller","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"329","published-online":{"date-parts":[[2021,8,24]]},"reference":[{"key":"uf5007_bb1","doi-asserted-by":"crossref","first-page":"210","DOI":"10.3201\/eid2402.160122","volume":"24","author":"Abedi","year":"2018","journal-title":"Emerg. 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