1m15: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1m15]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M15 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1m15]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M15 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M15 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginine_kinase Arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3 2.7.3.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginine_kinase Arginine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3 2.7.3.3] </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=1m15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m15 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m15 RCSB], [http://www.ebi.ac.uk/pdbsum/1m15 PDBsum]</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=1m15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m15 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1m15 RCSB], [http://www.ebi.ac.uk/pdbsum/1m15 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Arginine kinase]] | [[Category: Arginine kinase]] | ||
[[Category: Limulus polyphemus]] | [[Category: Limulus polyphemus]] | ||
[[Category: Chapman, M S | [[Category: Chapman, M S]] | ||
[[Category: Fabiola, F | [[Category: Fabiola, F]] | ||
[[Category: Gattis, J L | [[Category: Gattis, J L]] | ||
[[Category: Somasundaram, T | [[Category: Somasundaram, T]] | ||
[[Category: Yousef, M S | [[Category: Yousef, M S]] | ||
[[Category: Adenosine triphosphate]] | [[Category: Adenosine triphosphate]] | ||
[[Category: Creatine kinase]] | [[Category: Creatine kinase]] | ||
[[Category: Phosphagen kinase]] | [[Category: Phosphagen kinase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Transition state analog]] | [[Category: Transition state analog]] | ||
Revision as of 20:07, 5 January 2015
Transition state structure of arginine kinaseTransition state structure of arginine kinase
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights.,Yousef MS, Fabiola F, Gattis JL, Somasundaram T, Chapman MS Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2009-17. Epub 2002, Nov 23. PMID:12454458[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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