| Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni. | |
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MedLine Citation:
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PMID: 22403005 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Phosphoglycerate kinase (PGK) is indispensable during glycolysis for anaerobic glucose degradation and energy generation. Here we present comprehensive structure analysis of two putative PGKs from Bacillus anthracis str. Sterne and Campylobacter jejuni in the context of their structural homologs. They are the first PGKs from pathogenic bacteria reported in the Protein Data Bank. The crystal structure of PGK from Bacillus anthracis str. Sterne (BaPGK) has been determined at 1.68 Å while the structure of PGK from Campylobacter jejuni (CjPGK) has been determined at 2.14 Å resolution. The proteins' monomers are composed of two domains, each containing a Rossmann fold, hinged together by a helix which can be used to adjust the relative position between two domains. It is also shown that apo-forms of both BaPGK and CjPGK adopt open conformations as compared to the substrate and ATP bound forms of PGK from other species. |
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Authors:
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Heping Zheng; Ekaterina V Filippova; Karolina L Tkaczuk; Piotr Dworzynski; Maksymilian Chruszcz; Przemyslaw J Porebski; Zdzislaw Wawrzak; Olena Onopriyenko; Marina Kudritska; Sarah Grimshaw; Alexei Savchenko; Wayne F Anderson; Wladek Minor |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-3-10 |
Journal Detail:
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Title: Journal of structural and functional genomics Volume: - ISSN: 1570-0267 ISO Abbreviation: - Publication Date: 2012 Mar |
Date Detail:
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Created Date: 2012-3-9 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101128185 Medline TA: J Struct Funct Genomics Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Department of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA, 22908, USA. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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