2czq

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(New page: 200px<br /><applet load="2czq" size="350" color="white" frame="true" align="right" spinBox="true" caption="2czq, resolution 1.05&Aring;" /> '''A novel cutinase-lik...)
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[[Image:2czq.gif|left|200px]]<br /><applet load="2czq" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2czq, resolution 1.05&Aring;" />
 
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'''A novel cutinase-like protein from Cryptococcus sp.'''<br />
 
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==About this Structure==
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==A novel cutinase-like protein from Cryptococcus sp.==
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2CZQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cryptococcus_sp. Cryptococcus sp.] with <scene name='pdbligand=CIT:'>CIT</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CZQ OCA].
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<StructureSection load='2czq' size='340' side='right'caption='[[2czq]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
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[[Category: Cryptococcus sp.]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[2czq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptococcus_sp._S-2 Cryptococcus sp. S-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CZQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CZQ FirstGlance]. <br>
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[[Category: Iefuji, H.]]
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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]] 1.05&#8491;</td></tr>
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[[Category: Ikeda, H.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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[[Category: Kamini, N.R.]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2czq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2czq OCA], [https://pdbe.org/2czq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2czq RCSB], [https://www.ebi.ac.uk/pdbsum/2czq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2czq ProSAT]</span></td></tr>
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[[Category: Kondo, H.]]
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</table>
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[[Category: Masaki, K.]]
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== Function ==
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[[Category: Suzuki, M.]]
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[https://www.uniprot.org/uniprot/Q874E9_9TREE Q874E9_9TREE]
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[[Category: Tsuda, S.]]
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== Evolutionary Conservation ==
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[[Category: CIT]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: EDO]]
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Check<jmol>
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[[Category: alpha/beta hydrolase fold]]
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cz/2czq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2czq ConSurf].
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<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 structural and enzymatic characteristics of a cutinase-like enzyme (CLE) from Cryptococcus sp. strain S-2, which exhibits remote homology to a lipolytic enzyme and a cutinase from the fungus Fusarium solani (FS cutinase), were compared to investigate the unique substrate specificity of CLE. The crystal structure of CLE was solved to a 1.05 A resolution. Moreover, hydrolysis assays demonstrated the broad specificity of CLE for short and long-chain substrates, as well as the preferred specificity of FS cutinase for short-chain substrates. In addition, site-directed mutagenesis was performed to increase the hydrolysis activity on long-chain substrates, indicating that the hydrophobic aromatic residues are important for the specificity to the long-chain substrate. These results indicate that hydrophobic residues, especially the aromatic ones exposed to solvent, are important for retaining lipase activity.
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:51:35 2008''
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Crystal structure and enhanced activity of a cutinase-like enzyme from Cryptococcus sp. strain S-2.,Kodama Y, Masaki K, Kondo H, Suzuki M, Tsuda S, Nagura T, Shimba N, Suzuki E, Iefuji H Proteins. 2009 Nov 15;77(3):710-7. PMID:19544571<ref>PMID:19544571</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 2czq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Cryptococcus sp. S-2]]
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[[Category: Large Structures]]
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[[Category: Iefuji H]]
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[[Category: Ikeda H]]
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[[Category: Kamini NR]]
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[[Category: Kondo H]]
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[[Category: Masaki K]]
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[[Category: Suzuki M]]
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[[Category: Tsuda S]]

Current revision

A novel cutinase-like protein from Cryptococcus sp.

PDB ID 2czq

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