1m15: Difference between revisions

Revision as of 14:50, 21 February 2008

TRANSITION STATE STRUCTURE OF ARGININE KINASE

OverviewOverview

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.

About this StructureAbout this Structure

1M15 is a Single protein structure of sequence from Limulus polyphemus with , , and as ligands. Active as Transferase, with EC number 2.7.3.3. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 13:50:23 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:1m15.gif|left|200px]]<br /><applet load="1m15" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1m15.gif|left|200px]]<br /><applet load="1m15" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1m15, resolution 1.20&Aring;" />
 '''TRANSITION STATE STRUCTURE OF ARGININE KINASE'''<br />
 ==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 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.
 ==About this Structure==
-M15 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].
+M15 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 <scene name='pdbligand=NO3:'>NO3</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ARG:'>ARG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1M15 OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Transferase]]
-[[Category: Chapman, M.S.]]
+[[Category: Chapman, M S.]]
 [[Category: Fabiola, F.]]
-[[Category: Gattis, J.L.]]
+[[Category: Gattis, J L.]]
 [[Category: Somasundaram, T.]]
-[[Category: Yousef, M.S.]]
+[[Category: Yousef, M S.]]
 [[Category: ADP]]
 [[Category: ARG]]
@@ Line 29: / Line 29: @@
 [[Category: transition state analog]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:03:14 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:23 2008''