1xnb
From Proteopedia
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[[Image:1xnb.png|left|200px]] | [[Image:1xnb.png|left|200px]] | ||
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{{STRUCTURE_1xnb| PDB=1xnb | SCENE= }} | {{STRUCTURE_1xnb| PDB=1xnb | SCENE= }} | ||
===HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS=== | ===HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS=== | ||
+ | {{ABSTRACT_PUBMED_008890913}} | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[1xnb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XNB OCA]. | |
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+ | ==Reference== | ||
+ | <ref group="xtra">PMID:008890913</ref><ref group="xtra">PMID:011880627</ref><ref group="xtra">PMID:014695246</ref><references group="xtra"/> | ||
[[Category: Bacillus circulans]] | [[Category: Bacillus circulans]] | ||
[[Category: Endo-1,4-beta-xylanase]] | [[Category: Endo-1,4-beta-xylanase]] | ||
[[Category: Campbell, R L.]] | [[Category: Campbell, R L.]] | ||
[[Category: Glycosidase]] | [[Category: Glycosidase]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:14:14 2009'' |
Revision as of 13:12, 5 January 2013
HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF THE CATALYSIS
Template:ABSTRACT PUBMED 008890913
About this Structure
1xnb is a 1 chain structure with sequence from Bacillus circulans. Full crystallographic information is available from OCA.
Reference
- Krengel U, Dijkstra BW. Three-dimensional structure of Endo-1,4-beta-xylanase I from Aspergillus niger: molecular basis for its low pH optimum. J Mol Biol. 1996 Oct 18;263(1):70-8. PMID:8890913 doi:http://dx.doi.org/10.1006/jmbi.1996.0556
- Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. PMID:11880627 doi:10.1073/pnas.052706099
- Sandelin E. On hydrophobicity and conformational specificity in proteins. Biophys J. 2004 Jan;86(1 Pt 1):23-30. PMID:14695246 doi:10.1016/S0006-3495(04)74080-1