1nhc

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{{STRUCTURE_1nhc| PDB=1nhc | SCENE= }}
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'''Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger'''
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===Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger===
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==Overview==
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Endopolygalacturonase I is a processive enzyme, while the 60% sequence identical endopolygalacturonase II is not. The 1.70 A resolution crystal structure of endopolygalacturonase I reveals a narrowed substrate binding cleft. In addition, Arg96, a residue in this cleft previously shown to be critical for processivity, interacts with the substrate mimics glycerol and sulfate in several well-defined conformations in the six molecules in the asymmetric unit. From this we conclude that both Arg96 and the narrowed substrate binding cleft contribute to retaining the substrate while it moves through the active site after a cleavage event has occurred.
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(as it appears on PubMed at http://www.pubmed.gov), where 14623112 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14623112}}
==About this Structure==
==About this Structure==
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[[Category: Snijder, H J.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:49:42 2008''

Revision as of 01:49, 28 July 2008

Image:1nhc.png

Template:STRUCTURE 1nhc

Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger

Template:ABSTRACT PUBMED 14623112

About this Structure

1NHC is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.

Reference

Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger., van Pouderoyen G, Snijder HJ, Benen JA, Dijkstra BW, FEBS Lett. 2003 Nov 20;554(3):462-6. PMID:14623112

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