4n4q: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | ==Crystal Structure of N-acetylneuraminate lyase from Mycoplasma synoviae, crystal form II== | ||
<StructureSection load='4n4q' size='340' side='right' caption='[[4n4q]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4n4q]] is a 4 chain structure. 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> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n4p|4n4p]]</td></tr> | |||
<tr><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><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://www.rcsb.org/pdb/explore.do?structureId=4n4q RCSB], [http://www.ebi.ac.uk/pdbsum/4n4q PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24813614</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: N-acetylneuraminate lyase]] | |||
[[Category: Bracher, A.]] | |||
[[Category: Engen, J R.]] | |||
[[Category: Georgescauld, F.]] | |||
[[Category: Gupta, A J.]] | |||
[[Category: Hartl, F U.]] | |||
[[Category: Hayer-Hartl, M.]] | |||
[[Category: Popova, K.]] | |||
[[Category: Lyase]] | |||
[[Category: Tim barrel]] | |||
Revision as of 08:58, 21 May 2014
Crystal Structure of N-acetylneuraminate lyase from Mycoplasma synoviae, crystal form II
| ||||||||||||
