1uu4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,097 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,097 edits
No edit summary
Line 1: Line 1:
[[Image:1uu4.jpg|left|200px]]
{{Seed}}
[[Image:1uu4.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1uu4|  PDB=1uu4  |  SCENE=  }}  
{{STRUCTURE_1uu4|  PDB=1uu4  |  SCENE=  }}  


'''X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH CELLOBIOSE'''
===X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH CELLOBIOSE===




==Overview==
<!--
As part of an ongoing enzyme discovery program to investigate the properties and catalytic mechanism of glycoside hydrolase family 12 (GH 12) endoglucanases, a GH family that contains several cellulases that are of interest in industrial applications, we have solved four new crystal structures of wild-type Humicola grisea Cel12A in complexes formed by soaking with cellobiose, cellotetraose, cellopentaose, and a thio-linked cellotetraose derivative (G2SG2). These complex structures allow mapping of the non-covalent interactions between the enzyme and the glucosyl chain bound in subsites -4 to +2 of the enzyme, and shed light on the mechanism and function of GH 12 cellulases. The unhydrolysed cellopentaose and the G2SG2 cello-oligomers span the active site of the catalytically active H.grisea Cel12A enzyme, with the pyranoside bound in subsite -1 displaying a S31 skew boat conformation. After soaking in cellotetraose, the cello-oligomer that is found bound in site -4 to -1 contains a beta-1,3-linkage between the two cellobiose units in the oligomer, which is believed to have been formed by a transglycosylation reaction that has occurred during the ligand soak of the protein crystals. The close fit of this ligand and the binding sites occupied suggest a novel mixed beta-glucanase activity for this enzyme.
The line below this paragraph, {{ABSTRACT_PUBMED_15364577}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15364577 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15364577}}


==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Ligand complex]]
[[Category: Ligand complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:41:40 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:09:44 2008''

Revision as of 09:09, 28 July 2008

File:1uu4.png

Template:STRUCTURE 1uu4

X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH CELLOBIOSE

Template:ABSTRACT PUBMED 15364577

About this Structure

1UU4 is a Single protein structure of sequence from Humicola grisea. Full crystallographic information is available from OCA.

Reference

Crystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A., Sandgren M, Berglund GI, Shaw A, Stahlberg J, Kenne L, Desmet T, Mitchinson C, J Mol Biol. 2004 Oct 1;342(5):1505-17. PMID:15364577

Page seeded by OCA on Mon Jul 28 12:09:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1uu4&oldid=697852"