2oxb
From Proteopedia
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|PDB= 2oxb |SIZE=350|CAPTION= <scene name='initialview01'>2oxb</scene>, resolution 2.60Å | |PDB= 2oxb |SIZE=350|CAPTION= <scene name='initialview01'>2oxb</scene>, resolution 2.60Å | ||
|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+660'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+A+680'>AC2</scene> and <scene name='pdbsite=AC3:Suc+Binding+Site+For+Residue+A+845'>AC3</scene> | |SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+660'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+A+680'>AC2</scene> and <scene name='pdbsite=AC3:Suc+Binding+Site+For+Residue+A+845'>AC3</scene> | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SUC:SUCROSE'>SUC</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-fructofuranosidase Beta-fructofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.26 3.2.1.26] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-fructofuranosidase Beta-fructofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.26 3.2.1.26] </span> |
|GENE= ATBFRUCT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | |GENE= ATBFRUCT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2ac1|2AC1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oxb OCA], [http://www.ebi.ac.uk/pdbsum/2oxb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oxb RCSB]</span> | ||
}} | }} | ||
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[[Category: Rabijns, A.]] | [[Category: Rabijns, A.]] | ||
[[Category: Roy, K Le.]] | [[Category: Roy, K Le.]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: SUC]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:24:33 2008'' |
Revision as of 01:24, 31 March 2008
| |||||||
| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , | ||||||
| Gene: | ATBFRUCT1 (Arabidopsis thaliana) | ||||||
| Activity: | Beta-fructofuranosidase, with EC number 3.2.1.26 | ||||||
| Related: | 2AC1
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a cell-wall invertase (E203Q) from Arabidopsis thaliana in complex with sucrose
Overview
In the present study, we report on the X-ray crystallographic structure of a GH32 invertase mutant, (i.e., the Arabidopsis thaliana cell-wall invertase 1-E203Q, AtcwINV1-mutant) in complex with sucrose. This structure was solved to reveal the features of sugar binding in the catalytic pocket. However, as demonstrated by the X-ray structure the sugar binding and the catalytic pocket arrangement is significantly altered as compared with what was expected based on previous X-ray structures on GH-J clan enzymes. We performed a series of docking and molecular dynamics simulations on various derivatives of AtcwINV1 to reveal the reasons behind this modified sugar binding. Our results demonstrate that the E203Q mutation introduced into the catalytic pocket triggers conformational changes that alter the wild type substrate binding. In addition, this study also reveals the putative productive sucrose binding modus in the wild type enzyme. Proteins 2007. (c) 2007 Wiley-Liss, Inc.
About this Structure
2OXB is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study., Matrai J, Lammens W, Jonckheer A, Le Roy K, Rabijns A, Van den Ende W, De Maeyer M, Proteins. 2007 Oct 26;. PMID:17963237
Page seeded by OCA on Mon Mar 31 04:24:33 2008
