6p3l

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Current revision (14:53, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6p3l' size='340' side='right'caption='[[6p3l]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
<StructureSection load='6p3l' size='340' side='right'caption='[[6p3l]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6p3l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mychd Mychd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P3L FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6p3l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_hassiacum_DSM_44199 Mycolicibacterium hassiacum DSM 44199]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P3L 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=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.571&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ksi, C731_3354, MHAS_03236 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1122247 MYCHD])</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=GAI:GUANIDINE'>GAI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Steroid_Delta-isomerase Steroid Delta-isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.1 5.3.3.1] </span></td></tr>
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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=6p3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p3l OCA], [https://pdbe.org/6p3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p3l RCSB], [https://www.ebi.ac.uk/pdbsum/6p3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p3l 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=6p3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p3l OCA], [https://pdbe.org/6p3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p3l RCSB], [https://www.ebi.ac.uk/pdbsum/6p3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p3l ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/K5BJ73_MYCHD K5BJ73_MYCHD]
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The mechanisms that underly the adaptation of enzyme activities and stabilities to temperature are fundamental to our understanding of molecular evolution and how enzymes work. Here, we investigate the molecular and evolutionary mechanisms of enzyme temperature adaption, combining deep mechanistic studies with comprehensive sequence analyses of thousands of enzymes. We show that temperature adaptation in ketosteroid isomerase (KSI) arises primarily from one residue change with limited, local epistasis, and we establish the underlying physical mechanisms. This residue change occurs in diverse KSI backgrounds, suggesting parallel adaptation to temperature. We identify residues associated with organismal growth temperature across 1005 diverse bacterial enzyme families, suggesting widespread parallel adaptation to temperature. We assess the residue properties, molecular interactions, and interaction networks that appear to underly temperature adaptation.
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Parallel molecular mechanisms for enzyme temperature adaptation.,Pinney MM, Mokhtari DA, Akiva E, Yabukarski F, Sanchez DM, Liang R, Doukov T, Martinez TJ, Babbitt PC, Herschlag D Science. 2021 Mar 5;371(6533). pii: 371/6533/eaay2784. doi:, 10.1126/science.aay2784. PMID:33674467<ref>PMID:33674467</ref>
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==See Also==
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*[[Ketosteroid Isomerase|Ketosteroid Isomerase]]
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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 6p3l" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mychd]]
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[[Category: Mycolicibacterium hassiacum DSM 44199]]
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[[Category: Steroid Delta-isomerase]]
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[[Category: Doukov T]]
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[[Category: Doukov, T]]
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[[Category: Herschlag D]]
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[[Category: Herschlag, D]]
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[[Category: Pinney M]]
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[[Category: Pinney, M]]
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[[Category: Yabukarski F]]
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[[Category: Yabukarski, F]]
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[[Category: Isomerase]]
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[[Category: Thermophile]]
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Current revision

Crystal Structure of Ketosteroid Isomerase from Mycobacterium hassiacum (mhKSI)

PDB ID 6p3l

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