4pi2: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pi2]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylocystis_sp._ATCC_49242 Methylocystis sp. ATCC 49242]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PI2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4pi2]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylocystis_sp._ATCC_49242 Methylocystis sp. ATCC 49242]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PI2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.33Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4pi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pi2 OCA], [https://pdbe.org/4pi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pi2 RCSB], [https://www.ebi.ac.uk/pdbsum/4pi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pi2 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=4pi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pi2 OCA], [https://pdbe.org/4pi2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pi2 RCSB], [https://www.ebi.ac.uk/pdbsum/4pi2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pi2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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==See Also== | ==See Also== | ||
*[[Methane monooxygenase|Methane monooxygenase]] | *[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 03:44, 28 December 2023
Crystal structure of particulate methane monooxygenase from Methylocystis sp. ATCC 49242 (Rockwell) soaked in zincCrystal structure of particulate methane monooxygenase from Methylocystis sp. ATCC 49242 (Rockwell) soaked in zinc
Structural highlights
Publication Abstract from PubMedParticulate methane monooxygenase (pMMO) is a membrane-bound metalloenzyme that oxidizes methane to methanol in methanotrophic bacteria. Zinc is a known inhibitor of pMMO, but the details of zinc binding and the mechanism of inhibition are not understood. Metal binding and activity assays on membrane-bound pMMO from Methylococcus capsulatus (Bath) reveal that zinc inhibits pMMO at two sites that are distinct from the copper active site. The 2.6 A resolution crystal structure of Methylocystis species strain Rockwell pMMO reveals two previously undetected bound lipids, and metal soaking experiments identify likely locations for the two zinc inhibition sites. The first is the crystallographic zinc site in the pmoC subunit, and zinc binding here leads to ordering of 10 previously unobserved residues. A second zinc site is present on the cytoplasmic side of the pmoC subunit. Parallels between these results and zinc inhibition studies of several respiratory complexes suggest that zinc might inhibit proton transfer in pMMO. Effects of Zinc on Particulate Methane Monooxygenase Activity and Structure.,Sirajuddin S, Barupala D, Helling S, Marcus K, Stemmler TL, Rosenzweig AC J Biol Chem. 2014 Jun 18. pii: jbc.M114.581363. PMID:24942740[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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