2hnk

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Current revision (13:52, 13 March 2024) (edit) (undo)
 
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<StructureSection load='2hnk' size='340' side='right'caption='[[2hnk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='2hnk' size='340' side='right'caption='[[2hnk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2hnk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"leptospira_icteroides"_noguchi_1919 "leptospira icteroides" noguchi 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HNK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2hnk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptospira_interrogans Leptospira interrogans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HNK 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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 2.3&#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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2hnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hnk OCA], [https://pdbe.org/2hnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hnk RCSB], [https://www.ebi.ac.uk/pdbsum/2hnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hnk 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=2hnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hnk OCA], [https://pdbe.org/2hnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hnk RCSB], [https://www.ebi.ac.uk/pdbsum/2hnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hnk ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8F8Y3_LEPIN Q8F8Y3_LEPIN]
== 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=2hnk 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=2hnk 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 S-adenosylmethionine (SAM)-dependent O-methyltransferase from Leptospira interrogans (LiOMT) expressed by gene LA0415 belongs to the Methyltransf_3 family (Pfam PF01596). In this family all of the five bacterial homologues with known function are reported as SAM-dependent O-methylstransferases involved in antibiotic production. The crystal structure of LiOMT in complex with S-adenosylhomocysteine reported here is the first bacterial protein structure in this family. The LiOMT structure shows a conserved SAM-binding region and a probable metal-dependent catalytic site. The molecules of LiOMT generate homodimers by N-terminal swapping, which assists the pre-organization of the substrate-binding site. Based on the sequence and structural analysis, it is implied by the catalytic and substrate-binding site that the substrate of LiOMT is a phenolic derivative, which probably has a large ring-shaped moiety.
 
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Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans.,Hou X, Wang Y, Zhou Z, Bao S, Lin Y, Gong W J Struct Biol. 2007 Sep;159(3):523-8. Epub 2007 Apr 30. PMID:17561415<ref>PMID:17561415</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 2hnk" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]]
*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Leptospira icteroides noguchi 1919]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gong, W]]
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[[Category: Leptospira interrogans]]
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[[Category: Hou, X]]
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[[Category: Gong W]]
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[[Category: Wei, Z]]
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[[Category: Hou X]]
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[[Category: Modified rossman fold]]
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[[Category: Wei Z]]
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[[Category: Transferase]]
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Current revision

Crystal structure of SAM-dependent O-methyltransferase from pathogenic bacterium Leptospira interrogans

PDB ID 2hnk

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