1om0
From Proteopedia
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|PDB= 1om0 |SIZE=350|CAPTION= <scene name='initialview01'>1om0</scene>, resolution 1.80Å | |PDB= 1om0 |SIZE=350|CAPTION= <scene name='initialview01'>1om0</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1om0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1om0 OCA], [http://www.ebi.ac.uk/pdbsum/1om0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1om0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Roussel, A.]] | [[Category: Roussel, A.]] | ||
[[Category: Williamson, G.]] | [[Category: Williamson, G.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: NDG]] | ||
[[Category: beta-alpha barrel]] | [[Category: beta-alpha barrel]] | ||
| - | ''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 22:47:07 2008'' |
Revision as of 19:47, 30 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal structure of xylanase inhibitor protein (XIP-I) from wheat
Overview
A novel class of proteinaceous inhibitors exhibiting specificity towards microbial xylanases has recently been discovered in cereals. The three-dimensional structure of xylanase inhibitor protein I (XIP-I) from wheat (Triticum aestivum, var. Soisson) was determined by X-ray crystallography at 1.8 A (1 A=0.1 nm) resolution. The inhibitor possesses a (beta/alpha)(8) barrel fold and has structural features typical of glycoside hydrolase family 18, namely two consensus regions, approximately corresponding to the third and fourth barrel strands, and two non-proline cis -peptide bonds, Ser(36)-Phe and Trp(256)-Asp (in XIP-I numbering). However, detailed structural analysis of XIP-I revealed several differences in the region homologous with the active site of chitinases. The catalytic glutamic acid residue of family 18 chitinases [Glu(127) in hevamine, a chitinase/lysozyme from the rubber tree (Hevea brasiliensis)] is conserved in the structure of the inhibitor (Glu(128)), but its side chain is fully engaged in salt bridges with two neighbouring arginine residues. Gly(81), located in subsite -1 of hevamine, where the reaction intermediate is formed, is replaced by Tyr(80) in XIP-I. The tyrosine side chain fills the subsite area and makes a strong hydrogen bond with the side chain of Glu(190) located at the opposite side of the cleft, preventing access of the substrate to the catalytic glutamic acid. The structural differences in the inhibitor cleft structure probably account for the lack of activity of XIP-I towards chitin.
About this Structure
1OM0 is a Single protein structure of sequence from Triticum aestivum. Full crystallographic information is available from OCA.
Reference
Structural analysis of xylanase inhibitor protein I (XIP-I), a proteinaceous xylanase inhibitor from wheat (Triticum aestivum, var. Soisson)., Payan F, Flatman R, Porciero S, Williamson G, Juge N, Roussel A, Biochem J. 2003 Jun 1;372(Pt 2):399-405. PMID:12617724
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