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==Tricarbonylmanganese(I)-lysozyme complex : a structurally characterized organometallic protein== | |||
<StructureSection load='2q0m' size='340' side='right'caption='[[2q0m]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2q0m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q0M FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TFS:TRIFLUOROMETHANESULFONIC+ACID'>TFS</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=2q0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q0m OCA], [https://pdbe.org/2q0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q0m RCSB], [https://www.ebi.ac.uk/pdbsum/2q0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q0m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q0/2q0m_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2q0m ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The reaction of the new and structurally characterized covalent {Mn(CO)(3)(H(2)O)(2)}(+)-lysozyme adduct with NiS(4) and NiN(2)S(2) complexes generates binuclear Ni-Mn complexes; relevance to the reactivity of the protein-bound {Fe(CO)(CN)(2)} intermediate during maturation of [NiFe] hydrogenases is discussed. | |||
Tricarbonylmanganese(I)-lysozyme complex: a structurally characterized organometallic protein.,Razavet M, Artero V, Cavazza C, Oudart Y, Lebrun C, Fontecilla-Camps JC, Fontecave M Chem Commun (Camb). 2007 Jul 19;(27):2805-7. Epub 2007 Jun 11. PMID:17609782<ref>PMID:17609782</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2q0m" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Artero V]] | |||
[[Category: Artero | [[Category: Cavazza C]] | ||
[[Category: Cavazza | [[Category: Fontecave M]] | ||
[[Category: Fontecave | [[Category: Fontecilla-Camps JC]] | ||
[[Category: Fontecilla-Camps | [[Category: Oudart Y]] | ||
[[Category: Oudart | [[Category: Razavet M]] | ||
[[Category: Razavet | |||
Latest revision as of 11:31, 30 October 2024
Tricarbonylmanganese(I)-lysozyme complex : a structurally characterized organometallic proteinTricarbonylmanganese(I)-lysozyme complex : a structurally characterized organometallic protein
Structural highlights
FunctionLYSC_CHICK Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1] 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 PubMedThe reaction of the new and structurally characterized covalent {Mn(CO)(3)(H(2)O)(2)}(+)-lysozyme adduct with NiS(4) and NiN(2)S(2) complexes generates binuclear Ni-Mn complexes; relevance to the reactivity of the protein-bound {Fe(CO)(CN)(2)} intermediate during maturation of [NiFe] hydrogenases is discussed. Tricarbonylmanganese(I)-lysozyme complex: a structurally characterized organometallic protein.,Razavet M, Artero V, Cavazza C, Oudart Y, Lebrun C, Fontecilla-Camps JC, Fontecave M Chem Commun (Camb). 2007 Jul 19;(27):2805-7. Epub 2007 Jun 11. PMID:17609782[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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