1nof

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[[Image:1nof.gif|left|200px]]<br /><applet load="1nof" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nof.gif|left|200px]]
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caption="1nof, resolution 1.42&Aring;" />
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'''THE FIRST CRYSTALLOGRAPHIC STRUCTURE OF A XYLANASE FROM GLYCOSYL HYDROLASE FAMILY 5: IMPLICATIONS FOR CATALYSIS'''<br />
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{{Structure
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|PDB= 1nof |SIZE=350|CAPTION= <scene name='initialview01'>1nof</scene>, resolution 1.42&Aring;
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|SITE= <scene name='pdbsite=ACI:Catalytic+Acid/Base'>ACI</scene> and <scene name='pdbsite=NUC:Catalytic+Nucleophile'>NUC</scene>
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|LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8]
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|GENE= xynA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=556 Erwinia chrysanthemi])
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}}
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'''THE FIRST CRYSTALLOGRAPHIC STRUCTURE OF A XYLANASE FROM GLYCOSYL HYDROLASE FAMILY 5: IMPLICATIONS FOR CATALYSIS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Known structural/functional Sites: <scene name='pdbsite=ACI:Catalytic+Acid/Base'>ACI</scene> and <scene name='pdbsite=NUC:Catalytic+Nucleophile'>NUC</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOF OCA].
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1NOF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOF OCA].
==Reference==
==Reference==
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First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis., Larson SB, Day J, Barba de la Rosa AP, Keen NT, McPherson A, Biochemistry. 2003 Jul 22;42(28):8411-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12859186 12859186]
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First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis., Larson SB, Day J, Barba de la Rosa AP, Keen NT, McPherson A, Biochemistry. 2003 Jul 22;42(28):8411-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12859186 12859186]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Erwinia chrysanthemi]]
[[Category: Erwinia chrysanthemi]]
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[[Category: xylanase]]
[[Category: xylanase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:59:30 2008''

Revision as of 10:59, 20 March 2008


PDB ID 1nof

Drag the structure with the mouse to rotate
, resolution 1.42Å
Sites: and
Ligands:
Gene: xynA (Erwinia chrysanthemi)
Activity: Endo-1,4-beta-xylanase, with EC number 3.2.1.8
Coordinates: save as pdb, mmCIF, xml



THE FIRST CRYSTALLOGRAPHIC STRUCTURE OF A XYLANASE FROM GLYCOSYL HYDROLASE FAMILY 5: IMPLICATIONS FOR CATALYSIS


Overview

The room-temperature structure of xylanase (EC 3.2.1.8) from the bacterial plant pathogen Erwinia chrysanthemi expressed in Escherichia coli, a 45 kDa, 413-amino acid protein belonging to glycoside hydrolase family 5, has been determined by multiple isomorphous replacement and refined to a resolution of 1.42 A. This represents the first structure of a xylanase not belonging to either glycoside hydrolase family 10 or family 11. The enzyme is composed of two domains similar to most family 10 xylanases and the alpha-amylases. The catalytic domain (residues 46-315) has a (beta/alpha)(8)-barrel motif with a binding cleft along the C-terminal side of the beta-barrel. The catalytic residues, Glu165 and Glu253, determined by correspondence to other family 5 and family 10 glycoside hydrolases, lie inside this cleft on the C-terminal ends of beta-strands 4 and 7, respectively, with an O(epsilon)2...O(epsilon)1 distance of 4.22 A. The smaller domain (residues 31-43 and 323-413) has a beta(9)-barrel motif with five of the strands interfacing with alpha-helices 7 and 8 of the catalytic domain. The first 13 N-terminal residues form one beta-strand of this domain. Residues 44, 45, and 316-322 form the linkers between this domain and the catalytic domain.

About this Structure

1NOF is a Single protein structure of sequence from Erwinia chrysanthemi. Full crystallographic information is available from OCA.

Reference

First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis., Larson SB, Day J, Barba de la Rosa AP, Keen NT, McPherson A, Biochemistry. 2003 Jul 22;42(28):8411-22. PMID:12859186

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