5z0y

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'''Unreleased structure'''
 
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The entry 5z0y is ON HOLD until Paper Publication
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==Crystallization and structure determination of cytoplasm serine hydroxymethyltransferase (SHMT) from Pichia pastoris==
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<StructureSection load='5z0y' size='340' side='right' caption='[[5z0y]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5z0y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z0Y FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5z0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z0y OCA], [http://pdbe.org/5z0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z0y RCSB], [http://www.ebi.ac.uk/pdbsum/5z0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z0y ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/F2QZA4_KOMPC F2QZA4_KOMPC]] Interconversion of serine and glycine.[RuleBase:RU000585]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Serine hydroxymethyltransferase (SHMT) catalyzes the interconversion of serine and glycine, which is crucial for one carbon metabolism. Here, we report the first crystal structure of cytoplasmic SHMT from Pichia pastoris (pcSHMT) diffracted to 2.5A resolution in space group C2221. PcSHMT was a contaminant with our target protein expressed in Pichia pastoris and confirmed by mass spectrometry. The overall structure of pcSHMT is similar to Human mitochondrial SHMT and different to E. coli SHMT. Interestingly, the oligomerization of pcSHMT expressed in eukaryotic or prokaryotic system differs significantly and is regulated by pyridoxal-5'-phosphate. Our results revealed a close evolutionary relationship between Pichia pastoris and Human mitochondria.
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Authors: Chen, Z.Z., Zhang, M.F.
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Structure and function of cytoplasmic serine hydroxymethyltransferase from Pichia pastoris.,Zhang M, Wu W, Chen Z Biochem Biophys Res Commun. 2018 Feb 5;496(2):753-757. doi:, 10.1016/j.bbrc.2018.01.084. Epub 2018 Jan 12. PMID:29339156<ref>PMID:29339156</ref>
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Description: Crystallization and structure determination of cytoplasm serine hydroxymethyltransferase (SHMT) from Pichia pastoris
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Zhang, M.F]]
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<div class="pdbe-citations 5z0y" style="background-color:#fffaf0;"></div>
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[[Category: Chen, Z.Z]]
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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: Glycine hydroxymethyltransferase]]
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[[Category: Chen, Z]]
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[[Category: Zhang, M]]
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[[Category: Cytoplasm serine hydroxymethyltransferase]]
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[[Category: Pichia pastori]]
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[[Category: Shmt]]
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[[Category: Transferase]]

Revision as of 06:28, 14 March 2018

Crystallization and structure determination of cytoplasm serine hydroxymethyltransferase (SHMT) from Pichia pastoris

5z0y, resolution 2.50Å

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