1m15: Difference between revisions

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-[[Image:1m15.gif|left|200px]]
+{{Seed}}
+[[Image:1m15.png|left|200px]]
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 {{STRUCTURE_1m15|  PDB=1m15  |  SCENE=  }}
-'''TRANSITION STATE STRUCTURE OF ARGININE KINASE'''
+===TRANSITION STATE STRUCTURE OF ARGININE KINASE===
-==Overview==
+<!--
-The three-dimensional crystal structure of an arginine kinase transition-state analogue complex has been refined at 1.2 A resolution, with an overall R factor of 12.3%. The current model provides a unique opportunity to analyze the structure of a bimolecular (phosphagen kinase) enzyme in its transition state. This atomic resolution structure confirms in-line transfer of the phosphoryl group and the catalytic importance of the precise alignment of the substrates. The structure is consistent with a concerted proton transfer that has been proposed for an unrelated kinase. Refinement of anisotropic temperature factors and translation-libration-screw (TLS) analyses led to the identification of four rigid groups and their prevalent modes of motion in the transition state. The relative magnitudes of the mobility of rigid groups are consistent with their proposed roles in catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_12454458}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12454458 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12454458}}
 ==About this Structure==
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 [[Category: Phosphagen kinase]]
 [[Category: Transition state analog]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:30:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 22:59:29 2008''