2ayh

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[[Image:2ayh.jpg|left|200px]]<br /><applet load="2ayh" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ayh.jpg|left|200px]]
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caption="2ayh, resolution 1.6&Aring;" />
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'''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)'''<br />
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{{Structure
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|PDB= 2ayh |SIZE=350|CAPTION= <scene name='initialview01'>2ayh</scene>, resolution 1.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73]
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|GENE=
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}}
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'''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)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2AYH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hibberdia Hibberdia] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1AYH. Active as [http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYH OCA].
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2AYH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hibberdia Hibberdia]. This structure supersedes the now removed PDB entry 1AYH. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYH OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7588726 7588726]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/7588726 7588726]
[[Category: Hibberdia]]
[[Category: Hibberdia]]
[[Category: Licheninase]]
[[Category: Licheninase]]
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[[Category: hydrolase (glucanase)]]
[[Category: hydrolase (glucanase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:55:23 2008''

Revision as of 13:55, 20 March 2008


PDB ID 2ayh

Drag the structure with the mouse to rotate
, resolution 1.6Å
Ligands:
Activity: Licheninase, with EC number 3.2.1.73
Coordinates: save as pdb, mmCIF, xml



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 > 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. & 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.

About this Structure

2AYH is a Single protein structure of sequence from Hibberdia. 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

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