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[[Image:1zm1.gif|left|200px]]


{{Structure
==Crystal structures of complex F. succinogenes 1,3-1,4-beta-D-glucanase and beta-1,3-1,4-cellotriose==
|PDB= 1zm1 |SIZE=350|CAPTION= <scene name='initialview01'>1zm1</scene>, resolution 2.30&Aring;
<StructureSection load='1zm1' size='340' side='right'caption='[[1zm1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
<table><tr><td colspan='2'>[[1zm1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fibrobacter_succinogenes Fibrobacter succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZM1 FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zm1 OCA], [https://pdbe.org/1zm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zm1 RCSB], [https://www.ebi.ac.uk/pdbsum/1zm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zm1 ProSAT]</span></td></tr>
|RELATEDENTRY=[[1mve|1MVE]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zm1 OCA], [http://www.ebi.ac.uk/pdbsum/1zm1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zm1 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/GUB_FIBSS GUB_FIBSS]
== 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/zm/1zm1_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=1zm1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase (Fsbeta-glucanase) catalyzes the specific hydrolysis of beta-1,4 glycosidic bonds adjacent to beta-1,3 linkages in beta-D-glucans or lichenan. This is the first report to elucidate the crystal structure of a truncated Fsbeta-glucanase (TFsbeta-glucanase) in complex with beta-1,3-1,4-cellotriose, a major product of the enzyme reaction. The crystal structures, at a resolution of 2.3 angstroms, reveal that the overall fold of TFsbeta-glucanase remains virtually unchanged upon sugar binding. The enzyme accommodates five glucose residues, forming a concave active cleft. The beta-1,3-1,4-cellotriose with subsites -3 to -1 bound to the active cleft of TFsbeta-glucanase with its reducing end subsite -1 close to the key catalytic residues Glu56 and Glu60. All three subsites of the beta-1,3-1,4-cellotriose adopted a relaxed C(1)4 conformation, with a beta-1,3 glycosidic linkage between subsites -2 and -1, and a beta-1,4 glycosidic linkage between subsites -3 and -2. On the basis of the enzyme-product complex structure observed in this study, a catalytic mechanism and substrate binding conformation of the active site of TFsbeta-glucanase is proposed.


'''Crystal structures of complex F. succinogenes 1,3-1,4-beta-D-glucanase and beta-1,3-1,4-cellotriose'''
Crystal structure of truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase in complex with beta-1,3-1,4-cellotriose.,Tsai LC, Shyur LF, Cheng YS, Lee SH J Mol Biol. 2005 Dec 2;354(3):642-51. Epub 2005 Sep 30. PMID:16246371<ref>PMID:16246371</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1zm1" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase (Fsbeta-glucanase) catalyzes the specific hydrolysis of beta-1,4 glycosidic bonds adjacent to beta-1,3 linkages in beta-D-glucans or lichenan. This is the first report to elucidate the crystal structure of a truncated Fsbeta-glucanase (TFsbeta-glucanase) in complex with beta-1,3-1,4-cellotriose, a major product of the enzyme reaction. The crystal structures, at a resolution of 2.3 angstroms, reveal that the overall fold of TFsbeta-glucanase remains virtually unchanged upon sugar binding. The enzyme accommodates five glucose residues, forming a concave active cleft. The beta-1,3-1,4-cellotriose with subsites -3 to -1 bound to the active cleft of TFsbeta-glucanase with its reducing end subsite -1 close to the key catalytic residues Glu56 and Glu60. All three subsites of the beta-1,3-1,4-cellotriose adopted a relaxed C(1)4 conformation, with a beta-1,3 glycosidic linkage between subsites -2 and -1, and a beta-1,4 glycosidic linkage between subsites -3 and -2. On the basis of the enzyme-product complex structure observed in this study, a catalytic mechanism and substrate binding conformation of the active site of TFsbeta-glucanase is proposed.
*[[Glucanase 3D structures|Glucanase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1ZM1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Fibrobacter_succinogenes Fibrobacter succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZM1 OCA].
__TOC__
 
</StructureSection>
==Reference==
Crystal structure of truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase in complex with beta-1,3-1,4-cellotriose., Tsai LC, Shyur LF, Cheng YS, Lee SH, J Mol Biol. 2005 Dec 2;354(3):642-51. Epub 2005 Sep 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16246371 16246371]
[[Category: Fibrobacter succinogenes]]
[[Category: Fibrobacter succinogenes]]
[[Category: Licheninase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Cheng YS]]
[[Category: Cheng, Y S.]]
[[Category: Lee SH]]
[[Category: Lee, S H.]]
[[Category: Shyur LF]]
[[Category: Shyur, L F.]]
[[Category: Tsai LC]]
[[Category: Tsai, L C.]]
[[Category: active cleft]]
[[Category: beta-1,3-1,4-cellotriose (cltr)]]
[[Category: glucanase/1,3-1,4-beta-d-glucanase]]
 
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