1nof: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1nof.gif|left|200px]]
{{Seed}}
[[Image:1nof.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nof|  PDB=1nof  |  SCENE=  }}  
{{STRUCTURE_1nof|  PDB=1nof  |  SCENE=  }}  


'''THE FIRST CRYSTALLOGRAPHIC STRUCTURE OF A XYLANASE FROM GLYCOSYL HYDROLASE FAMILY 5: IMPLICATIONS FOR CATALYSIS'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_12859186}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12859186 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12859186}}


==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Glycohydrolase family 5]]
[[Category: Glycohydrolase family 5]]
[[Category: Xylanase]]
[[Category: Xylanase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:46:47 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:26:03 2008''

Revision as of 02:26, 28 July 2008

File:1nof.png

Template:STRUCTURE 1nof

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

Template:ABSTRACT PUBMED 12859186

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

Page seeded by OCA on Mon Jul 28 05:26:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1nof&oldid=683216"