1gzj

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1gzj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GZJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1gzj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GZJ FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</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=1gzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gzj OCA], [https://pdbe.org/1gzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gzj RCSB], [https://www.ebi.ac.uk/pdbsum/1gzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gzj ProSAT]</span></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=1gzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gzj OCA], [https://pdbe.org/1gzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gzj RCSB], [https://www.ebi.ac.uk/pdbsum/1gzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gzj ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8TG26_THEAU Q8TG26_THEAU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1gzj ConSurf].
</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=1gzj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The crystal structure of Thermoascus aurantiacus endoglucanase (Cel5A), a family 5 glycoside hydrolase, has been determined to 1.62 A resolution by multiple isomorphous replacement with anomalous scattering. It is the first report of a structure in the subfamily to which Cel5A belongs. Cel5A consists solely of a catalytic module with compact eight-fold beta/alpha barrel architecture. The length of the tryptophan-rich substrate binding groove suggests the presence of substrate binding subsites -4 to +3. Structural comparison shows that two glycines are completely conserved in the family, in addition to the two catalytic glutamates and six other conserved residues previously identified. Gly 44 in particular is part of a type IV C-terminal helix capping motif, whose disruption is likely to affect the position of an essential conserved arginine. One aromatic residue (Trp 170 in Cel5A), not conserved in term of sequence, is nonetheless spatially conserved in the substrate binding groove. Its role might be to force the bend that occurs in the polysaccharide chain on binding, thus favoring substrate distortion at subsite -1.
 
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The 1.62 A structure of Thermoascus aurantiacus endoglucanase: completing the structural picture of subfamilies in glycoside hydrolase family 5.,Lo Leggio L, Larsen S FEBS Lett. 2002 Jul 17;523(1-3):103-8. PMID:12123813<ref>PMID:12123813</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1gzj" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cellulase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thermoascus aurantiacus]]
[[Category: Thermoascus aurantiacus]]
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[[Category: Larsen, S]]
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[[Category: Larsen S]]
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[[Category: Leggio, L Lo]]
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[[Category: Lo Leggio L]]
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[[Category: Pickersgill, R W]]
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[[Category: Pickersgill RW]]
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[[Category: Family 5]]
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[[Category: Glycoside hydrolase]]
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[[Category: Hydrolase]]
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Revision as of 11:26, 27 March 2024

Structure of Thermoascus aurantiacus family 5 endoglucanase

PDB ID 1gzj

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