1mkv: Difference between revisions

Revision as of 00:13, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mkv.png

Template:STRUCTURE 1mkv

CARBOXYLIC ESTER HYDROLASE COMPLEX (PLA2 + TRANSITION STATE ANALOG COMPLEX)CARBOXYLIC ESTER HYDROLASE COMPLEX (PLA2 + TRANSITION STATE ANALOG COMPLEX)

Template:ABSTRACT PUBMED 9761900

About this StructureAbout this Structure

1MKV is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the complex of bovine pancreatic phospholipase A2 with a transition-state analogue., Sekar K, Kumar A, Liu X, Tsai MD, Gelb MH, Sundaralingam M, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):334-41. PMID:9761900

Page seeded by OCA on Thu Jul 3 00:13:13 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1mkv.gif|left|200px]]
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 {{STRUCTURE_1mkv|  PDB=1mkv  |  SCENE=  }}
-'''CARBOXYLIC ESTER HYDROLASE COMPLEX (PLA2 + TRANSITION STATE ANALOG COMPLEX)'''
+===CARBOXYLIC ESTER HYDROLASE COMPLEX (PLA2 + TRANSITION STATE ANALOG COMPLEX)===
-==Overview==
+<!--
-The 1.89 A resolution structure of the complex of bovine pancreatic phospholipase A2 (PLA2) with the transition-state analogue L-1-O-octyl-2-heptylphosphonyl-sn-glycero-3-phosphoethanolamine (TSA) has been determined. The crystal of the complex is trigonal, space group P3121, a = b = 46.58 and c = 102.91 A and isomorphous to the native recombinant wild type (WT). The structure was refined to a final crystallographic R value of 18.0% including 957 protein atoms, 88 water molecules, one calcium ion and all 31 non-H atoms of the inhibitor at 1.89 A resolution. In all, 7 726 reflections [F&gt;2sigma(F)] were used between 8.0 and 1.89 A resolution. The inhibitor is deeply locked into the active-site cleft and coordinates to the calcium ion by displacing the two water molecules in the calcium pentagonal bipyramid by the anionic O atoms of the phosphate and phosphonate group. The hydroxyl group of Tyr69 hydrogen bonds to the second anionic O atom of the phosphate group while that of the phosphonate group replaces the third water, 'catalytic' water, which forms a hydrogen bond to Ndelta1 of His48. The fourth water which also shares Ndelta1 of His48 is displaced by the steric hinderance of the inhibitor. The fifth conserved structural water is still present in the active site and forms a network of hydrogen bonds with the surrounding residues. The structure is compared to the other known TSA-PLA2 complexes.
+The line below this paragraph, {{ABSTRACT_PUBMED_9761900}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9761900 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9761900}}
 ==About this Structure==
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 [[Category: Enzyme]]
 [[Category: Hydrolase]]
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