The structure of BVU2987 from Bacteroides vulgatus reveals a superfamily of bacterial periplasmic proteins with possible inhibitory function
Proteins that contain the DUF2874 domain constitute a new Pfam family PF11396. Members of this family have predominantly been identified in microbes found in the human gut and oral cavity. The crystal structure of one member of this family, BVU2987 from Bacteroides vulgatus, has been determined, rev...
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Published in: | Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 66; no. 10; pp. 1265 - 1273 |
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Main Authors: | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
5 Abbey Square, Chester, Cheshire CH1 2HU, England
International Union of Crystallography
01-10-2010
Wiley Subscription Services, Inc |
Subjects: | |
Online Access: | Get full text |
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Summary: | Proteins that contain the DUF2874 domain constitute a new Pfam family PF11396. Members of this family have predominantly been identified in microbes found in the human gut and oral cavity. The crystal structure of one member of this family, BVU2987 from Bacteroides vulgatus, has been determined, revealing a β‐lactamase inhibitor protein‐like structure with a tandem repeat of domains. Sequence analysis and structural comparisons reveal that BVU2987 and other DUF2874 proteins are related to β‐lactamase inhibitor protein, PepSY and SmpA_OmlA proteins and hence are likely to function as inhibitory proteins. |
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Bibliography: | ark:/67375/WNG-CM88WM1D-R ArticleID:AYF2WD5118 istex:1044ABFF35571225AB4992D298A56D22B95E4544 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 AC02-76SF00515; U54 GM074898; WT077044/Z/05/Z USDOE Office of Science (SC), Basic Energy Sciences (BES) National Institutes of Health (NIH) USDOE Office of Science (SC), Biological and Environmental Research (BER) National Center for Research Resources (NCRR) Wellcome Trust National Institute of General Medical Sciences (NIGMS) These authors contributed equally to this work. |
ISSN: | 1744-3091 1744-3091 2053-230X |
DOI: | 10.1107/S1744309109046788 |