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4eyz
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of an uncommon cellulosome-related protein module from Ruminococcus flavefaciens that resembles papain-like cysteine peptidases== | |
| - | + | <StructureSection load='4eyz' size='340' side='right' caption='[[4eyz]], [[Resolution|resolution]] 1.38Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4eyz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ruminococcus_flavefaciens Ruminococcus flavefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EYZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EYZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NlpC/P60_2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1265 Ruminococcus flavefaciens])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4eyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eyz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eyz RCSB], [http://www.ebi.ac.uk/pdbsum/4eyz PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | BACKGROUND: is one of the predominant fiber-degrading bacteria found in the rumen of herbivores. Bioinformatic analysis of the recently sequenced genome indicated that this bacterium produces one of the most intricate cellulosome systems known to date. A distinct ORF, encoding for a multi-modular protein, RflaF_05439, was discovered during mining of the genome sequence. It is composed of two tandem modules of currently undefined function that share 45% identity and a C-terminal X-dockerin modular dyad. Gaining insight into the diversity, architecture and organization of different types of proteins in the cellulosome system is essential for broadening our understanding of a multi-enzyme complex, considered to be one of the most efficient systems for plant cell wall polysaccharide degradation in nature. METHODOLOGYPRINCIPAL FINDINGS: Following bioinformatic analysis, the second tandem module of RflaF_05439 was cloned and its selenium-labeled derivative was expressed and crystallized. The crystals belong to space group P2 with unit-cell parameters of = 65.81, = 60.61, = 66.13 A, beta = 107.66 degrees and contain two protein molecules in the asymmetric unit. The crystal structure was determined at 1.38-A resolution by X-ray diffraction using the single-wavelength anomalous dispersion (SAD) method and was refined to R and R of 0.127 and 0.152 respectively. The protein molecule mainly comprises a beta-sheet flanked by short alpha-helixes, and a globular alpha-helical domain. The structure was found to be structurally similar to members of the NlpC/P60 superfamily of cysteine peptidases. CONCLUSIONSSIGNIFICANCE: The 3D structure of the second repeat of the RflaF_05439 enabled us to propose a role for the currently undefined function of this protein. Its putative function as a cysteine peptidase is inferred from structural homology studies. It is therefore apparent that cellulosomes integrate proteins with other functions in addition to the classic well-defined carbohydrate active enzymes. | ||
| - | + | Crystal Structure of an Uncommon Cellulosome-Related Protein Module from Ruminococcus flavefaciens That Resembles Papain-Like Cysteine Peptidases.,Levy-Assaraf M, Voronov-Goldman M, Rozman Grinberg I, Weiserman G, Shimon LJ, Jindou S, Borovok I, White BA, Bayer EA, Lamed R, Frolow F PLoS One. 2013;8(2):e56138. doi: 10.1371/journal.pone.0056138. Epub 2013 Feb 14. PMID:23457513<ref>PMID:23457513</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ruminococcus flavefaciens]] | [[Category: Ruminococcus flavefaciens]] | ||
| - | [[Category: Bayer, E | + | [[Category: Bayer, E]] |
| - | [[Category: Frolow, F | + | [[Category: Frolow, F]] |
| - | [[Category: Lamed, R | + | [[Category: Lamed, R]] |
| - | [[Category: Voronov-Goldman, M | + | [[Category: Voronov-Goldman, M]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Putative protease]] | [[Category: Putative protease]] | ||
Revision as of 11:50, 21 December 2014
Crystal structure of an uncommon cellulosome-related protein module from Ruminococcus flavefaciens that resembles papain-like cysteine peptidases
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