1glh

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[[Image:1glh.gif|left|200px]]
[[Image:1glh.gif|left|200px]]
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{{Structure
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|PDB= 1glh |SIZE=350|CAPTION= <scene name='initialview01'>1glh</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1glh", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_1glh| PDB=1glh | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1glh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glh OCA], [http://www.ebi.ac.uk/pdbsum/1glh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1glh RCSB]</span>
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}}
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'''CATION BINDING TO A BACILLUS (1,3-1,4)-BETA-GLUCANASE. GEOMETRY, AFFINITY AND EFFECT ON PROTEIN STABILITY'''
'''CATION BINDING TO A BACILLUS (1,3-1,4)-BETA-GLUCANASE. GEOMETRY, AFFINITY AND EFFECT ON PROTEIN STABILITY'''
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[[Category: Heinemann, U.]]
[[Category: Heinemann, U.]]
[[Category: Keitel, T.]]
[[Category: Keitel, T.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:43:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:46:36 2008''
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Revision as of 14:43, 2 May 2008

Image:1glh.gif

Template:STRUCTURE 1glh

CATION BINDING TO A BACILLUS (1,3-1,4)-BETA-GLUCANASE. GEOMETRY, AFFINITY AND EFFECT ON PROTEIN STABILITY


Overview

The hybrid Bacillus (1,3-1,4)-beta-glucanase H(A16-M), consisting of 16 N-terminal amino acids derived from the mature form of the B. amyloliquefaciens enzyme and of 198 C-proximal amino acids from the B. macerans enzyme, binds a calcium ion at a site at its molecular surface remote from the active center [T. Keitel, O. Simon, R. Borriss & U. Heinemann (1993) Proc. Natl Acad. Sci. USA 90, 5287-5291]. X-ray diffraction analysis at 0.22-nm resolution of crystals grown in the absence of calcium and in the presence of EDTA shows this site to be occupied by a sodium ion. Whereas the calcium ion has six oxygen atoms in its coordination sphere, two of which are from water molecules, sodium is fivefold coordinated with a fifth ligand belonging to a symmetry-related protein molecule in the crystal lattice. The affinity of H(A16-M) for calcium over sodium has been determined calorimetrically. Calcium binding stabilizes the native three-dimensional structure of the protein as shown by guanidinium chloride unfolding and thermal inactivation experiments. The enhanced enzymic activity of Bacillus beta-glucanases at elevated temperatures in the presence of calcium ions is attributed to a general stabilizing effect by the cation.

About this Structure

1GLH is a Single protein structure of sequence from Synthetic construct. Full crystallographic information is available from OCA.

Reference

Cation binding to a Bacillus (1,3-1,4)-beta-glucanase. Geometry, affinity and effect on protein stability., Keitel T, Meldgaard M, Heinemann U, Eur J Biochem. 1994 May 15;222(1):203-14. PMID:8200344 Page seeded by OCA on Fri May 2 17:43:35 2008

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