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5j9a
From Proteopedia
(Difference between revisions)
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<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=5j9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j9a OCA], [http://pdbe.org/5j9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j9a RCSB], [http://www.ebi.ac.uk/pdbsum/5j9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j9a ProSAT]</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=5j9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j9a OCA], [http://pdbe.org/5j9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j9a RCSB], [http://www.ebi.ac.uk/pdbsum/5j9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j9a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Arginine kinase provides a model for functional dynamics, studied through crystallography, enzymology, and nuclear magnetic resonance. Structures are now solved, at ambient temperature, for the transition state analog (TSA) complex. Analysis of quasi-rigid sub-domain displacements show that differences between the two TSA structures average about 5% of changes between substrate-free and TSA forms, and they are nearly co-linear. Small backbone hinge rotations map to sites that also flex on substrate binding. Anisotropic atomic displacement parameters (ADPs) are refined using rigid-body TLS constraints. Consistency between crystal forms shows that they reflect intrinsic molecular properties more than crystal lattice effects. In many regions, the favored directions of thermal/static displacement are appreciably correlated with movements on substrate binding. Correlation between ADPs and larger substrate-associated movements implies that the latter approximately follow paths of low-energy intrinsic motions. | ||
| + | |||
| + | The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase.,Godsey MH, Davulcu O, Nix JC, Skalicky JJ, Bruschweiler RP, Chapman MS Structure. 2016 Sep 1. pii: S0969-2126(16)30224-6. doi:, 10.1016/j.str.2016.07.013. PMID:27594681<ref>PMID:27594681</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5j9a" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:31, 21 September 2016
Ambient temperature transition state structure of arginine kinase - crystal 11/Form II
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