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Structural organization of WrbA in apo-and holoprotein crystals
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SYSNO ASEP 0343396 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Structural organization of WrbA in apo-and holoprotein crystals Author(s) Wolfová, J. (CZ)
Kutá-Smatanová, Ivana (UEK-B) RID
Brynda, Jiří (UOCHB-X) RID, ORCID
Mesters, J. R. (DE)
Lapkouski, M. (CZ)
Kutý, Michal (UEK-B)
Natalello, A. (IT)
Chatterjee, N. (US)
Chern, S. Y. (US)
Ebbel, E. (US)
Ricci, A. (US)
Grandori, R. (IT)
Ettrich, Rüdiger (UEK-B) RID, ORCID, SAI
Carey, J. (US)Number of authors 14 Source Title Biochimica Et Biophysica Acta-Proteins and Proteomics. - : Elsevier - ISSN 1570-9639
Roč. 1794, č. 9 (2009), s. 1288-1298Number of pages 11 s. Language eng - English Country NL - Netherlands Keywords twisted open-sheet fold ; electrostatic potential surface ; dimerization ; trichloroacetic acid Subject RIV CC - Organic Chemistry R&D Projects LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z40550506 - UOCHB-X (2005-2011) AV0Z60870520 - UEK-B (2005-2011) UT WOS 000270100200002 DOI 10.1016/j.bbapap.2009.08.001 Annotation Crystal structure of /E. coli/ protein WrbA holoprotein to 2.6 and 2.0 Å resolution, and WrbA apoprotein to 1.85 Å, are refined and analysed comparatively through the lens of flavodoxin structures. The results indicate that differences between apo- and holoWrbA crystal structures are manifested on many levels of protein organization as well as in the FMN-binding sites. Structural changes upon cofactor binding are compared with the monomeric flavodoxins. Analysis of the three crystal structures described here, together with flavodoxin structures, rationalizes functional similarities and differences of the WrbAs relative to flavodoxins, leading to a new understanding of the defining features of WrbAs. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Year of Publishing 2011
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