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| | <StructureSection load='4n4q' size='340' side='right'caption='[[4n4q]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4n4q' size='340' side='right'caption='[[4n4q]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4n4q]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs5 Mycs5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N4Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N4Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4n4q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycoplasmopsis_synoviae_53 Mycoplasmopsis synoviae 53]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N4Q FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n4p|4n4p]]</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4q OCA], [https://pdbe.org/4n4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n4q RCSB], [https://www.ebi.ac.uk/pdbsum/4n4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4q ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MS53_0198, nanA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262723 MYCS5])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylneuraminate_lyase N-acetylneuraminate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.3 4.1.3.3] </span></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=4n4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4q OCA], [http://pdbe.org/4n4q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n4q RCSB], [http://www.ebi.ac.uk/pdbsum/4n4q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q4A6K4_MYCS5 Q4A6K4_MYCS5] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4n4q" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4n4q" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[N-acetylneuraminate lyase 3D structures|N-acetylneuraminate lyase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mycs5]] | + | [[Category: Mycoplasmopsis synoviae 53]] |
| - | [[Category: N-acetylneuraminate lyase]]
| + | [[Category: Bracher A]] |
| - | [[Category: Bracher, A]] | + | [[Category: Engen JR]] |
| - | [[Category: Engen, J R]] | + | [[Category: Georgescauld F]] |
| - | [[Category: Georgescauld, F]] | + | [[Category: Gupta AJ]] |
| - | [[Category: Gupta, A J]] | + | [[Category: Hartl FU]] |
| - | [[Category: Hartl, F U]] | + | [[Category: Hayer-Hartl M]] |
| - | [[Category: Hayer-Hartl, M]] | + | [[Category: Popova K]] |
| - | [[Category: Popova, K]] | + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Tim barrel]]
| + | |
| Structural highlights
Function
Q4A6K4_MYCS5
Publication Abstract from PubMed
The GroEL/ES chaperonin system functions as a protein folding cage. Many obligate substrates of GroEL share the (betaalpha)8 TIM-barrel fold, but how the chaperonin promotes folding of these proteins is not known. Here, we analyzed the folding of DapA at peptide resolution using hydrogen/deuterium exchange and mass spectrometry. During spontaneous folding, all elements of the DapA TIM barrel acquire structure simultaneously in a process associated with a long search time. In contrast, GroEL/ES accelerates folding more than 30-fold by catalyzing segmental structure formation in the TIM barrel. Segmental structure formation is also observed during the fast spontaneous folding of a structural homolog of DapA from a bacterium that lacks GroEL/ES. Thus, chaperonin independence correlates with folding properties otherwise enforced by protein confinement in the GroEL/ES cage. We suggest that folding catalysis by GroEL/ES is required by a set of proteins to reach native state at a biologically relevant timescale, avoiding aggregation or degradation.
GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding.,Georgescauld F, Popova K, Gupta AJ, Bracher A, Engen JR, Hayer-Hartl M, Hartl FU Cell. 2014 May 8;157(4):922-34. doi: 10.1016/j.cell.2014.03.038. PMID:24813614[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Georgescauld F, Popova K, Gupta AJ, Bracher A, Engen JR, Hayer-Hartl M, Hartl FU. GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding. Cell. 2014 May 8;157(4):922-34. doi: 10.1016/j.cell.2014.03.038. PMID:24813614 doi:http://dx.doi.org/10.1016/j.cell.2014.03.038
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