This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2ayh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ayh.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2ayh.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ayh| PDB=2ayh | SCENE= }}
{{STRUCTURE_2ayh| PDB=2ayh | SCENE= }}
-
'''CRYSTAL AND MOLECULAR STRUCTURE AT 1.6 ANGSTROMS RESOLUTION OF THE HYBRID BACILLUS ENDO-1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE H(A16-M)'''
+
===CRYSTAL AND MOLECULAR STRUCTURE AT 1.6 ANGSTROMS RESOLUTION OF THE HYBRID BACILLUS ENDO-1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE H(A16-M)===
-
==Overview==
+
<!--
-
H(A16-M) is a hybrid endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus. Its crystal structure was refined using synchrotron X-ray diffraction data up to a maximal resolution of 0.16 nm. The R value of the resulting model is 14.3% against 21,032 reflections &gt; 2 sigma. 93% of the amino acid residues are in the most favorable regions of the Ramachandran diagram, and geometrical parameters are in accordance with other proteins solved at high resolution. As shown earlier [Keitel, T., Simon, O., Borriss, R. &amp; Heinemann, U. (1993) Proc. Natl Acad. Sci. USA 90, 5287-5291], the protein folds into a compact jellyroll-type beta-sheet structure. A systematic analysis of the secondary structure reveals the presence of two major antiparallel beta-sheets and a three-stranded minor mixed sheet. Amino acid residues involved in catalysis and substrate binding are located inside a deep channel spanning the surface of the protein. To investigate the stereochemical cause of the observed specificity of endo-1,3-1,4-beta-D-glucan 4-glucanohydrolases towards beta-1,4 glycosyl bonds adjacent to beta-1,3 bonds, the high-resolution crystal structure has been used to model an enzyme-substrate complex. It is proposed that productive substrate binding to the subsites p1, p2 and p3 of H(A16-M) requires a beta-1,3 linkage between glucose units bound to p1 and p2.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7588726}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7588726 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7588726}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Heinemann, U.]]
[[Category: Heinemann, U.]]
[[Category: Keitel, T.]]
[[Category: Keitel, T.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:37:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 6 00:57:50 2008''

Revision as of 21:57, 5 July 2008

Template:STRUCTURE 2ayh

CRYSTAL AND MOLECULAR STRUCTURE AT 1.6 ANGSTROMS RESOLUTION OF THE HYBRID BACILLUS ENDO-1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE H(A16-M)

Template:ABSTRACT PUBMED 7588726

About this Structure

2AYH is a Single protein structure of sequence from Hybrid. This structure supersedes the now removed PDB entry 1ayh. Full crystallographic information is available from OCA.

Reference

Crystal and molecular structure at 0.16-nm resolution of the hybrid Bacillus endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase H(A16-M)., Hahn M, Keitel T, Heinemann U, Eur J Biochem. 1995 Sep 15;232(3):849-58. PMID:7588726

Page seeded by OCA on Sun Jul 6 00:57:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools