{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,13]],"date-time":"2026-04-13T21:10:05Z","timestamp":1776114605850,"version":"3.50.1"},"reference-count":41,"publisher":"Springer Science and Business Media LLC","issue":"1","content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["BMC Bioinformatics"],"published-print":{"date-parts":[[2014,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>Background<\/jats:title><jats:p>The Acel_2062 protein from<jats:italic>Acidothermus cellulolyticus<\/jats:italic>is a protein of unknown function. Initial sequence analysis predicted that it was a metallopeptidase from the presence of a motif conserved amongst the Asp-zincins, which are peptidases that contain a single, catalytic zinc ion ligated by the histidines and aspartic acid within the motif (<jats:bold>H<\/jats:bold>EXX<jats:bold>H<\/jats:bold>XXGXX<jats:bold>D<\/jats:bold>). The Acel_2062 protein was chosen by the Joint Center for Structural Genomics for crystal structure determination to explore novel protein sequence space and structure-based function annotation.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>The crystal structure confirmed that the Acel_2062 protein consisted of a single, zincin-like metallopeptidase-like domain. The Met-turn, a structural feature thought to be important for a Met-zincin because it stabilizes the active site, is absent, and its stabilizing role may have been conferred to the C-terminal Tyr113. In our crystallographic model there are two molecules in the asymmetric unit and from size-exclusion chromatography, the protein dimerizes in solution. A water molecule is present in the putative zinc-binding site in one monomer, which is replaced by one of two observed conformations of His95 in the other.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusions<\/jats:title><jats:p>The Acel_2062 protein is structurally related to the zincins. It contains the minimum structural features of a member of this protein superfamily, and can be described as a \u201cmini- zincin\u201d. There is a striking parallel with the structure of a mini-Glu-zincin, which represents the minimum structure of a Glu-zincin (a metallopeptidase in which the third zinc ligand is a glutamic acid). Rather than being an ancestral state, phylogenetic analysis suggests that the mini-zincins are derived from larger proteins.<\/jats:p><\/jats:sec>","DOI":"10.1186\/1471-2105-15-1","type":"journal-article","created":{"date-parts":[[2014,1,3]],"date-time":"2014-01-03T04:02:00Z","timestamp":1388721720000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":384,"title":["New mini- zincin structures provide a minimal scaffold for members of this metallopeptidase superfamily"],"prefix":"10.1186","volume":"15","author":[{"given":"Christine B","family":"Trame","sequence":"first","affiliation":[]},{"given":"Yuanyuan","family":"Chang","sequence":"additional","affiliation":[]},{"given":"Herbert L","family":"Axelrod","sequence":"additional","affiliation":[]},{"given":"Ruth Y","family":"Eberhardt","sequence":"additional","affiliation":[]},{"given":"Penelope","family":"Coggill","sequence":"additional","affiliation":[]},{"given":"Marco","family":"Punta","sequence":"additional","affiliation":[]},{"given":"Neil D","family":"Rawlings","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2014,1,3]]},"reference":[{"key":"6243_CR1","doi-asserted-by":"publisher","first-page":"823","DOI":"10.1002\/pro.5560040502","volume":"4","author":"W St\u00f6cker","year":"1995","unstructured":"St\u00f6cker W, Grams F, Baumann U, Reinemer P, Gomis-R\u00fcth FX, McKay DB, Bode W: The metzincins\u2013topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. 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