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New page: left|200px<br /><applet load="1glh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1glh, resolution 2.0Å" /> '''CATION BINDING TO A B...
 
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[[Image:1glh.gif|left|200px]]<br /><applet load="1glh" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1glh, resolution 2.0&Aring;" />
'''CATION BINDING TO A BACILLUS (1,3-1,4)-BETA-GLUCANASE. GEOMETRY, AFFINITY AND EFFECT ON PROTEIN STABILITY'''<br />


==Overview==
==CATION BINDING TO A BACILLUS (1,3-1,4)-BETA-GLUCANASE. GEOMETRY, AFFINITY AND EFFECT ON PROTEIN STABILITY==
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 &amp; 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.
<StructureSection load='1glh' size='340' side='right'caption='[[1glh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1glh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GLH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1glh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1glh OCA], [https://pdbe.org/1glh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1glh RCSB], [https://www.ebi.ac.uk/pdbsum/1glh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1glh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUB_PAEMA GUB_PAEMA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gl/1glh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1glh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 &amp; 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==
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<ref>PMID:8200344</ref>
1GLH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GLH OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8200344 8200344]
</div>
[[Category: Licheninase]]
<div class="pdbe-citations 1glh" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
 
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Synthetic construct]]
[[Category: Heinemann, U.]]
[[Category: Heinemann U]]
[[Category: Keitel, T.]]
[[Category: Keitel T]]
[[Category: NA]]
[[Category: hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:09:02 2007''

Latest revision as of 04:33, 17 October 2024

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

1glh, resolution 2.00Å

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