1m15: Difference between revisions

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==Transition state structure of arginine kinase==
==Transition state structure of arginine kinase==
<StructureSection load='1m15' size='340' side='right' caption='[[1m15]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
<StructureSection load='1m15' size='340' side='right'caption='[[1m15]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1m15]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atlantic_horseshoe_crab Atlantic horseshoe crab]. 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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1M15 FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</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 id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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://pdbe.org/1m15 PDBe], [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'>[https://proteopedia.org/fgij/fg.htm?mol=1m15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m15 OCA], [https://pdbe.org/1m15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m15 RCSB], [https://www.ebi.ac.uk/pdbsum/1m15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m15 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KARG_LIMPO KARG_LIMPO]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m15_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m15_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 17: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m15 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m15 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:12454458</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1m15" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Arginine kinase|Arginine kinase]]
*[[Arginine kinase 3D structures|Arginine kinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arginine kinase]]
[[Category: Large Structures]]
[[Category: Atlantic horseshoe crab]]
[[Category: Limulus polyphemus]]
[[Category: Chapman, M S]]
[[Category: Chapman MS]]
[[Category: Fabiola, F]]
[[Category: Fabiola F]]
[[Category: Gattis, J L]]
[[Category: Gattis JL]]
[[Category: Somasundaram, T]]
[[Category: Somasundaram T]]
[[Category: Yousef, M S]]
[[Category: Yousef MS]]
[[Category: Adenosine triphosphate]]
[[Category: Creatine kinase]]
[[Category: Phosphagen kinase]]
[[Category: Transferase]]
[[Category: Transition state analog]]

Latest revision as of 10:38, 14 February 2024

Transition state structure of arginine kinaseTransition state structure of arginine kinase

Structural highlights

1m15 is a 1 chain structure with sequence from Limulus polyphemus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KARG_LIMPO

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1m15, resolution 1.20Å

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