1azk: Difference between revisions

Revision as of 17:55, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1azk.png

Template:STRUCTURE 1azk

THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 19 STRUCTURESTHREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 19 STRUCTURES

Template:ABSTRACT PUBMED 9041630

About this StructureAbout this Structure

1AZK is a Single protein structure of sequence from Hypocrea jecorina. Full experimental information is available from OCA.

ReferenceReference

Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei., Mattinen ML, Kontteli M, Kerovuo J, Linder M, Annila A, Lindeberg G, Reinikainen T, Drakenberg T, Protein Sci. 1997 Feb;6(2):294-303. PMID:9041630

Page seeded by OCA on Mon Jun 30 17:55:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1azk.gif|left|200px]]
+{{Seed}}
+[[Image:1azk.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1azk|  PDB=1azk  |  SCENE=  }}
-'''THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 19 STRUCTURES'''
+===THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 19 STRUCTURES===
-==Overview==
+<!--
-Three-dimensional solution structures for three engineered, synthetic CBDs (Y5A, Y31A, and Y32A) of cellobiohydrolase I (CBHI) from Trichoderma reesei were studied with nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. According to CD measurements the antiparallel beta-sheet structure of the CBD fold was preserved in all engineered peptides. The three-dimensional NMR-based structures of Y31A and Y32A revealed only small local changes due to mutations in the flat face of CBD, which is expected to bind to crystalline cellulose. Therefore, the structural roles of Y31 and Y32 are minor, but their functional importance is obvious because these mutants do not bind strongly to cellulose. In the case of Y5A, the disruption of the structural framework at the N-terminus and the complete loss of binding affinity implies that Y5 has both structural and functional significance. The number of aromatic residues and their precise spatial arrangement in the flat face of the type I CBD fold appears to be critical for specific binding. A model for the CBD binding in which the three aligned aromatic rings stack onto every other glucose ring of the cellulose polymer is discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_9041630}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9041630 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9041630}}
 ==About this Structure==
-AZK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZK OCA].
+AZK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZK OCA].
 ==Reference==
@@ Line 30: / Line 34: @@
 [[Category: Nuclear magnetic resonance spectroscopy]]
 [[Category: Protein-carbohydrate interaction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:52:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:55:00 2008''