1uu6
From Proteopedia
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| - | [[Image:1uu6. | + | [[Image:1uu6.jpg|left|200px]]<br /><applet load="1uu6" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1uu6" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1uu6, resolution 1.40Å" /> | caption="1uu6, resolution 1.40Å" /> | ||
'''X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH A SOAKED CELLOPENTAOSE'''<br /> | '''X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH A SOAKED CELLOPENTAOSE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UU6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Humicola_grisea Humicola grisea] with PG4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] | + | 1UU6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Humicola_grisea Humicola grisea] with PG4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Known structural/functional Site: <scene name='pdbsite=AC1:Pg4 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UU6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ligand complex]] | [[Category: ligand complex]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:12:12 2007'' |
Revision as of 16:02, 18 December 2007
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X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH A SOAKED CELLOPENTAOSE
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.
About this Structure
1UU6 is a Single protein structure of sequence from Humicola grisea with PG4 as ligand. Active as Cellulase, with EC number 3.2.1.4 Known structural/functional Site: . 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
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