4n4p: Difference between revisions
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New page: '''Unreleased structure''' The entry 4n4p is ON HOLD Authors: Popova, K., Bracher, A. Description: Crystal Structure of N-acetylneuraminate lyase from Mycoplasma synoviae, crystal form... |
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The | ==Crystal Structure of N-acetylneuraminate lyase from Mycoplasma synoviae, crystal form I== | ||
<StructureSection load='4n4p' size='340' side='right'caption='[[4n4p]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4n4p]] 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=4N4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N4P FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=4n4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4p OCA], [https://pdbe.org/4n4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n4p RCSB], [https://www.ebi.ac.uk/pdbsum/4n4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4p ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q4A6K4_MYCS5 Q4A6K4_MYCS5] | |||
<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> | |||
<div class="pdbe-citations 4n4p" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[N-acetylneuraminate lyase 3D structures|N-acetylneuraminate lyase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycoplasmopsis synoviae 53]] | |||
[[Category: Bracher A]] | |||
[[Category: Engen JR]] | |||
[[Category: Georgescauld F]] | |||
[[Category: Gupta AJ]] | |||
[[Category: Hartl FU]] | |||
[[Category: Hayer-Hartl M]] | |||
[[Category: Popova K]] | |||
