1slv: Difference between revisions

Revision as of 16:26, 27 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:1slv.png

Template:STRUCTURE 1slv

RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUNDRAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUND

Template:ABSTRACT PUBMED 8634241

About this StructureAbout this Structure

1SLV is a Protein complex structure of sequences from Escherichia coli and Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structures of a designed binding site in trypsin show metal-dependent geometry., Brinen LS, Willett WS, Craik CS, Fletterick RJ, Biochemistry. 1996 May 14;35(19):5999-6009. PMID:8634241

Page seeded by OCA on Sun Jul 27 16:25:59 2008

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-'''RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUND'''
+===RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUND===
-==Overview==
+<!--
-The three-dimensional structures of complexes of trypsin N143H, E151H bound to ecotin A86H are determined at 2.0 A resolution via X-ray crystallography in the absence and presence of the transition metals Zn2+, Ni2+, and Cu2+. The binding site for these transition metals was constructed by substitution of key amino acids with histidine at the trypsin-ecotin interface in the S2'/P2' pocket. Three histidine side chains, two on trypsin at positions 143 and 151 and one on ecotin at position 86, anchor the metals and provide extended catalytic recognition for substrates with His in the P2' pocket. Comparisons of the three-dimensional structures show the different geometries that result upon the binding of metal in the engineered tridentate site and suggest a structural basis for the kinetics of the metal-regulated catalysis. Of the three metals, the binding of zinc results in the most favorable binding geometry, not dissimilar to those observed in naturally occurring zinc binding proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_8634241}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8634241 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8634241}}
 ==About this Structure==
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 [[Category: Protein engineering]]
 [[Category: Serine protease]]
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