1ukr: 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:1ukr.jpg|left|200px]]
{{Seed}}
[[Image:1ukr.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ukr|  PDB=1ukr  |  SCENE=  }}  
{{STRUCTURE_1ukr|  PDB=1ukr  |  SCENE=  }}  


'''STRUCTURE OF ENDO-1,4-BETA-XYLANASE C'''
===STRUCTURE OF ENDO-1,4-BETA-XYLANASE C===




==Overview==
<!--  
The crystal structure of endo-1,4-beta-xylanase I from Aspergillus niger has been solved by molecular replacement and was refined to 2.4 A resolution. The final R-factor for all data from 6 to 2.4 A is 17.9%. The A. niger xylanase has a characteristic fold which is unique for family G xylanases (root-mean-square deviation = 1.1 A to Trichoderma reesei xylanase I, which has 53% sequence identity). It consists of a single domain composed predominantly of beta-strands. Two beta-sheets are twisted around a deep, long cleft, which is lined with many aromatic amino acid residues and is large enough to accommodate at least four xylose residues. The two conserved glutamate residues, Glu79 and Glu170, which are likely to be involved in catalysis, reach into this cleft from opposite sides. A niger xylanase I is of particular commercial interest because of its low pH optimum. A model is proposed which explains this low pH optimum compared to other members of xylanase family G.
The line below this paragraph, {{ABSTRACT_PUBMED_8890913}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8890913 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8890913}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Signal]]
[[Category: Signal]]
[[Category: Xylan degradation]]
[[Category: Xylan degradation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:21:48 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:03:42 2008''

Revision as of 01:03, 28 July 2008

File:1ukr.png

Template:STRUCTURE 1ukr

STRUCTURE OF ENDO-1,4-BETA-XYLANASE C

Template:ABSTRACT PUBMED 8890913

About this Structure

1UKR is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus niger: molecular basis for its low pH optimum., Krengel U, Dijkstra BW, J Mol Biol. 1996 Oct 18;263(1):70-8. PMID:8890913

Page seeded by OCA on Mon Jul 28 04:03:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ukr&oldid=680192"