1mgp: Difference between revisions
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<StructureSection load='1mgp' size='340' side='right' caption='[[1mgp]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1mgp' size='340' side='right' caption='[[1mgp]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mgp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1mgp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MGP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MGP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<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=1mgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mgp RCSB], [http://www.ebi.ac.uk/pdbsum/1mgp PDBsum], [http://www.topsan.org/Proteins/BSGC/1mgp TOPSAN]</span></td></tr> | <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=1mgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgp OCA], [http://pdbe.org/1mgp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mgp RCSB], [http://www.ebi.ac.uk/pdbsum/1mgp PDBsum], [http://www.topsan.org/Proteins/BSGC/1mgp TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1mgp" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 43589]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Kim, R]] | [[Category: Kim, R]] |
Revision as of 18:27, 11 September 2015
Hypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding functionHypothetical protein TM841 from Thermotoga maritima reveals fatty acid binding function
Structural highlights
Function[Y1468_THEMA] Binds long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe determined the three-dimensional (3D) crystal structure of protein TM841, a protein product from a hypothetical open-reading frame in the genome of the hyperthermophile bacterium Thermotoga maritima, to 2.0 A resolution. The protein belongs to a large protein family, DegV or COG1307 of unknown function. The 35 kDa protein consists of two separate domains, with low-level structural resemblance to domains from other proteins with known 3D structures. These structural homologies, however, provided no clues for the function of TM841. But the electron density maps revealed clear density for a bound fatty-acid molecule in a pocket between the two protein domains. The structure indicates that TM841 has the molecular function of fatty-acid binding and may play a role in the cellular functions of fatty acid transport or metabolism. Crystal structure of a hypothetical protein, TM841 of Thermotoga maritima, reveals its function as a fatty acid-binding protein.,Schulze-Gahmen U, Pelaschier J, Yokota H, Kim R, Kim SH Proteins. 2003 Mar 1;50(4):526-30. PMID:12577257[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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