1hew: Difference between revisions

Revision as of 08:05, 1 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:1hew.png

Template:STRUCTURE 1hew

REFINEMENT OF AN ENZYME COMPLEX WITH INHIBITOR BOUND AT PARTIAL OCCUPANCY. HEN EGG-WHITE LYSOZYME AND TRI-N-ACETYLCHITOTRIOSE AT 1.75 ANGSTROMS RESOLUTIONREFINEMENT OF AN ENZYME COMPLEX WITH INHIBITOR BOUND AT PARTIAL OCCUPANCY. HEN EGG-WHITE LYSOZYME AND TRI-N-ACETYLCHITOTRIOSE AT 1.75 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1569548

About this StructureAbout this Structure

1HEW is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

Refinement of an enzyme complex with inhibitor bound at partial occupancy. Hen egg-white lysozyme and tri-N-acetylchitotriose at 1.75 A resolution., Cheetham JC, Artymiuk PJ, Phillips DC, J Mol Biol. 1992 Apr 5;224(3):613-28. PMID:1569548

Page seeded by OCA on Tue Jul 1 08:05:36 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1hew.gif|left|200px]]
+{{Seed}}
+[[Image:1hew.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1hew|  PDB=1hew  |  SCENE=  }}
-'''REFINEMENT OF AN ENZYME COMPLEX WITH INHIBITOR BOUND AT PARTIAL OCCUPANCY. HEN EGG-WHITE LYSOZYME AND TRI-N-ACETYLCHITOTRIOSE AT 1.75 ANGSTROMS RESOLUTION'''
+===REFINEMENT OF AN ENZYME COMPLEX WITH INHIBITOR BOUND AT PARTIAL OCCUPANCY. HEN EGG-WHITE LYSOZYME AND TRI-N-ACETYLCHITOTRIOSE AT 1.75 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The structure of the tri-N-acetylchitotriose inhibitor complex of hen egg-white lysozyme has been refined at 1.75 A resolution, using data collected from a complex crystal with ligand bound at less than full occupancy. To determine the exact value of the inhibitor occupancy, a model comprising unliganded and sugar-bound protein molecules was generated and refined against the 1.75 A data, using a modified version of the Hendrickson &amp; Konnert least-squares procedure. The crystallographic R-factor for the model was found to fall to a minimum at 55% bound sugar. Conventional refinement assuming unit occupancy was found to yield incorrect thermal and positional parameters. Application of the same refinement procedures to an earlier 2.0 A data set, collected independently on different complex crystals by Blake et al. gave less consistent results than the 1.75 A refinement. From an analysis of the high resolution structure a detailed picture of the protein-carbohydrate interactions in the non-productive complex has emerged, together with the conformation and mobility changes that accompany ligand binding. The specificity of interaction between the protein and inhibitor, bound in subsites A to C of the active site, is seen to be generated primarily by an extensive network of hydrogen bonds, both to the protein itself and to bound solvent molecules. The latter also play an important role in maintaining the structural integrity of the active site cleft in the apo-protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_1569548}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1569548 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1569548}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Cheetham, J C.]]
 [[Category: Phillips, D C.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:46:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 08:05:36 2008''