1fzi
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fzi]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FZI FirstGlance]. <br> | <table><tr><td colspan='2'>[[1fzi]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FZI FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=XE:XENON'>XE</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=1fzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fzi OCA], [https://pdbe.org/1fzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fzi RCSB], [https://www.ebi.ac.uk/pdbsum/1fzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fzi 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=1fzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fzi OCA], [https://pdbe.org/1fzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fzi RCSB], [https://www.ebi.ac.uk/pdbsum/1fzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fzi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/MEMA_METCA MEMA_METCA] Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 20: | Line 20: | ||
</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=1fzi 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=1fzi ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | To investigate the role of protein cavities in facilitating movement of the substrates, methane and dioxygen, in the soluble methane monooxygenase hydroxylase (MMOH), we determined the X-ray structures of MMOH from Methylococcus capsulatus (Bath) cocrystallized with dibromomethane or iodoethane, or by using crystals pressurized with xenon gas. The halogenated alkanes bind in two cavities within the alpha-subunit that extend from one surface of the protein to the buried dinuclear iron active site. Two additional binding sites were located in the beta-subunit. Pressurization of two crystal forms of MMOH with xenon resulted in the identification of six binding sites located exclusively in the alpha-subunit. These results indicate that hydrophobic species bind preferentially in preexisting cavities in MMOH and support the hypothesis that such cavities may play a functional role in sequestering and enhancing the availability of the physiological substrates for reaction at the active site. | ||
| - | |||
| - | Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase.,Whittington DA, Rosenzweig AC, Frederick CA, Lippard SJ Biochemistry. 2001 Mar 27;40(12):3476-82. PMID:11297413<ref>PMID:11297413</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1fzi" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Methane monooxygenase|Methane monooxygenase]] | + | *[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]] |
| - | + | ||
| - | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Methylococcus capsulatus]] | [[Category: Methylococcus capsulatus]] | ||
| - | [[Category: Frederick | + | [[Category: Frederick CA]] |
| - | [[Category: Lippard | + | [[Category: Lippard SJ]] |
| - | [[Category: Rosenzweig | + | [[Category: Rosenzweig AC]] |
| - | [[Category: Whittington | + | [[Category: Whittington DA]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
METHANE MONOOXYGENASE HYDROXYLASE, FORM I PRESSURIZED WITH XENON GAS
| |||||||||||
