2e67

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Current revision (13:49, 13 March 2024) (edit) (undo)
 
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<StructureSection load='2e67' size='340' side='right'caption='[[2e67]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='2e67' size='340' side='right'caption='[[2e67]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2e67]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E67 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2e67]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E67 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2e67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e67 OCA], [https://pdbe.org/2e67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e67 RCSB], [https://www.ebi.ac.uk/pdbsum/2e67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e67 ProSAT], [https://www.topsan.org/Proteins/RSGI/2e67 TOPSAN]</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=2e67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e67 OCA], [https://pdbe.org/2e67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e67 RCSB], [https://www.ebi.ac.uk/pdbsum/2e67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e67 ProSAT], [https://www.topsan.org/Proteins/RSGI/2e67 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/YDJC_THET8 YDJC_THET8]] Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides.<ref>PMID:18177738</ref>
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[https://www.uniprot.org/uniprot/YDJC_THET8 YDJC_THET8] Probably catalyzes the deacetylation of acetylated carbohydrates an important step in the degradation of oligosaccharides.<ref>PMID:18177738</ref>
== 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=2e67 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=2e67 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 YdjC-family protein is widely distributed, from human to bacteria, but so far no three-dimensional structure and functional analysis of this family of proteins has been reported. We determined the three-dimensional structure of the YdjC homolog TTHB029 at a resolution of 2.9A. The overall structure of the monomer consists of (betaalpha)-barrel fold forming a homodimer. Asp21, His60, and His127 residues coordinate to Mg(2+) as a possible active site. TTHB029 shows structural similarity to the peptidoglycan N-acetylglucosamine deacetylase from Streptococcus pneumoniae (SpPgdA). The active site groove of SpPgdA includes the Zn(2+) coordinated to Asp276, His326, and His330. Despite the low sequence identity, metal-binding residues of Asp-His-His were conserved among the two enzymes. There were definitive differences, however, in that one of the histidines of the metal-binding site was substituted for the other histidine located on the other loop. Moreover, these important metal-binding residues and the residues of the presumed active site are fully conserved in YdjC-family protein.
 
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Crystal structure of the YdjC-family protein TTHB029 from Thermus thermophilus HB8: structural relationship with peptidoglycan N-acetylglucosamine deacetylase.,Imagawa T, Iino H, Kanagawa M, Ebihara A, Kuramitsu S, Tsuge H Biochem Biophys Res Commun. 2008 Mar 14;367(3):535-41. Epub 2008 Jan 3. PMID:18177738<ref>PMID:18177738</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 2e67" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Thet8]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Imagawa, T]]
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[[Category: Imagawa T]]
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[[Category: Structural genomic]]
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[[Category: Hypothetical protein]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Rsgi]]
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[[Category: Unknown function]]
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Current revision

Crystal structure of the hypothetical protein TTHB029 from Thermus thermophilus HB8

PDB ID 2e67

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