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| - | [[Image:1om0.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1om0| PDB=1om0 | SCENE= }} | | {{STRUCTURE_1om0| PDB=1om0 | SCENE= }} |
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| - | '''crystal structure of xylanase inhibitor protein (XIP-I) from wheat'''
| + | ===crystal structure of xylanase inhibitor protein (XIP-I) from wheat=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12617724}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12617724 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12617724}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Williamson, G.]] | | [[Category: Williamson, G.]] |
| | [[Category: Beta-alpha barrel]] | | [[Category: Beta-alpha barrel]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:00:50 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:44:24 2008'' |
Revision as of 20:44, 28 July 2008
Template:STRUCTURE 1om0
crystal structure of xylanase inhibitor protein (XIP-I) from wheat
Template:ABSTRACT PUBMED 12617724
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
Page seeded by OCA on Mon Jul 28 23:44:24 2008
