1lu0: Difference between revisions

Revision as of 22:13, 2 July 2008

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File:1lu0.png

Template:STRUCTURE 1lu0

Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal CoordinationAtomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination

Template:ABSTRACT PUBMED 12198301

About this StructureAbout this Structure

1LU0 is a Single protein structure of sequence from Cucurbita maxima. Full crystallographic information is available from OCA.

ReferenceReference

Atomic resolution structure of squash trypsin inhibitor: unexpected metal coordination., Thaimattam R, Tykarska E, Bierzynski A, Sheldrick GM, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1448-61. Epub 2002, Aug 23. PMID:12198301

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

OCA

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 {{STRUCTURE_1lu0|  PDB=1lu0  |  SCENE=  }}
-'''Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination'''
+===Atomic Resolution Structure of Squash Trypsin Inhibitor: Unexpected Metal Coordination===
-==Overview==
+<!--
-CMTI-I, a small-protein trypsin inhibitor, has been crystallized as a 4:1 protein-zinc complex. The metal is coordinated in a symmetric tetrahedral fashion by glutamate/glutamic acid side chains. The structure was solved by direct methods in the absence of prior knowledge of the special position metal centre and refined with anisotropic displacement parameters using diffraction data extending to 1.03 A. In the final calculations, the main-chain atoms of low B(eq) values were refined without restraint control. The two molecules in the asymmetric unit have a conformation that is very similar to that reported earlier for CMTI-I in complex with trypsin, despite the Met8Leu mutation of the present variant. The only significant differences are in the enzyme-binding epitope (including the Arg5 residue) and in a higher mobility loop around Glu24. The present crystal structure contains organic solvent molecules (glycerol, MPD) that interact with the inhibitor molecules in an area that is at the enzyme-inhibitor interface in the CMTI-I-trypsin complex. A perfectly ordered residue (Ala18) has an unusual Ramachandran conformation as a result of geometrical strain introduced by the three disulfide bridges that clamp the protein fold. The results confirm deficiencies of some stereochemical restraints, such as peptide planarity or the N-C(alpha)-C angle, and suggest a link between their violations and hydrogen bonding.
+The line below this paragraph, {{ABSTRACT_PUBMED_12198301}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12198301}}
 ==About this Structure==
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 [[Category: Metal coordination]]
 [[Category: Serine protease inhibitor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:17:14 2008''
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