1nhc
From Proteopedia
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|PDB= 1nhc |SIZE=350|CAPTION= <scene name='initialview01'>1nhc</scene>, resolution 1.70Å | |PDB= 1nhc |SIZE=350|CAPTION= <scene name='initialview01'>1nhc</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Polygalacturonase Polygalacturonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.15 3.2.1.15] </span> | |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1czf|1CZF]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nhc OCA], [http://www.ebi.ac.uk/pdbsum/1nhc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nhc RCSB]</span> | ||
}} | }} | ||
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[[Category: Pouderoyen, G van.]] | [[Category: Pouderoyen, G van.]] | ||
[[Category: Snijder, H J.]] | [[Category: Snijder, H J.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: MAN]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: SO4]] | ||
[[Category: beta-helix]] | [[Category: beta-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:30:22 2008'' |
Revision as of 19:30, 30 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Activity: | Polygalacturonase, with EC number 3.2.1.15 | ||||||
| Related: | 1CZF
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural insights into the processivity of endopolygalacturonase I from Aspergillus niger
Overview
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.
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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