1m15: Difference between revisions

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New page: left|200px<br /><applet load="1m15" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m15, resolution 1.20Å" /> '''TRANSITION STATE STR...
 
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[[Image:1m15.gif|left|200px]]<br /><applet load="1m15" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1m15, resolution 1.20&Aring;" />
'''TRANSITION STATE STRUCTURE OF ARGININE KINASE'''<br />


==Overview==
==Transition state structure of arginine kinase==
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.
<StructureSection load='1m15' size='340' side='right'caption='[[1m15]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<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='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='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'>[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>
== Function ==
[https://www.uniprot.org/uniprot/KARG_LIMPO KARG_LIMPO]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


==About this Structure==
==See Also==
1M15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Limulus_polyphemus Limulus polyphemus] with NO3, MG, ARG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.3. 2.7.3.3.] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M15 OCA].
*[[Arginine kinase 3D structures|Arginine kinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12454458 12454458]
[[Category: Large Structures]]
[[Category: Limulus polyphemus]]
[[Category: Limulus polyphemus]]
[[Category: Single protein]]
[[Category: Chapman MS]]
[[Category: Transferase]]
[[Category: Fabiola F]]
[[Category: Chapman, M.S.]]
[[Category: Gattis JL]]
[[Category: Fabiola, F.]]
[[Category: Somasundaram T]]
[[Category: Gattis, J.L.]]
[[Category: Yousef MS]]
[[Category: Somasundaram, T.]]
[[Category: Yousef, M.S.]]
[[Category: ADP]]
[[Category: ARG]]
[[Category: MG]]
[[Category: NO3]]
[[Category: adenosine triphosphate]]
[[Category: arginine kinase]]
[[Category: creatine kinase]]
[[Category: phosphagen kinase]]
[[Category: transition state analog]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:03:14 2007''

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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