1h8v: Difference between revisions

Revision as of 06:50, 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:1h8v.png

Template:STRUCTURE 1h8v

THE X-RAY CRYSTAL STRUCTURE OF THE TRICHODERMA REESEI FAMILY 12 ENDOGLUCANASE 3, CEL12A, AT 1.9 A RESOLUTIONTHE X-RAY CRYSTAL STRUCTURE OF THE TRICHODERMA REESEI FAMILY 12 ENDOGLUCANASE 3, CEL12A, AT 1.9 A RESOLUTION

Template:ABSTRACT PUBMED 11327768

About this StructureAbout this Structure

1H8V is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.

ReferenceReference

The X-ray crystal structure of the Trichoderma reesei family 12 endoglucanase 3, Cel12A, at 1.9 A resolution., Sandgren M, Shaw A, Ropp TH, Wu S, Bott R, Cameron AD, Stahlberg J, Mitchinson C, Jones TA, J Mol Biol. 2001 Apr 27;308(2):295-310. PMID:11327768

Page seeded by OCA on Tue Jul 1 06:50:40 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1h8v.jpg|left|200px]]
+{{Seed}}
+[[Image:1h8v.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1h8v|  PDB=1h8v  |  SCENE=  }}
-'''THE X-RAY CRYSTAL STRUCTURE OF THE TRICHODERMA REESEI FAMILY 12 ENDOGLUCANASE 3, CEL12A, AT 1.9 A RESOLUTION'''
+===THE X-RAY CRYSTAL STRUCTURE OF THE TRICHODERMA REESEI FAMILY 12 ENDOGLUCANASE 3, CEL12A, AT 1.9 A RESOLUTION===
-==Overview==
+<!--
-We present the three-dimensional structure of Trichoderma reesei endoglucanase 3 (Cel12A), a small, 218 amino acid residue (24.5 kDa), neutral pI, glycoside hydrolase family 12 cellulase that lacks a cellulose-binding module. The structure has been determined using X-ray crystallography and refined to 1.9 A resolution. The asymmetric unit consists of six non-crystallographic symmetry-related molecules that were exploited to improve initial multiple isomorphous replacement phasing, and subsequent structure refinement. The enzyme contains one disulfide bridge and is glycosylated at Asp164 by a single N-acetyl glucosamine residue. The protein has the expected fold for a glycoside hydrolase clan-C family 12 enzyme. It contains two beta-sheets, of six and nine strands, packed on top of one another, and one alpha-helix. The concave surface of the nine-stranded beta-sheet forms a large substrate-binding groove in which the active-site residues are located. In the active site, we find a carboxylic acid trio, similar to that of glycoside hydrolase families 7 and 16. The strictly conserved Asp99 hydrogen bonds to the nucleophile, the invariant Glu116. The binding crevice is lined with both aromatic and polar amino acid side-chains which may play a role in substrate binding. The structure of the fungal family 12 enzyme presented here allows a complete structural characterization of the glycoside hydrolase-C clan.
+The line below this paragraph, {{ABSTRACT_PUBMED_11327768}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11327768 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11327768}}
 ==About this Structure==
@@ Line 39: / Line 43: @@
 [[Category: Hydrolase]]
 [[Category: Trichoderma reesei cel12a]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:34:51 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:50:40 2008''