6hih
From Proteopedia
(Difference between revisions)
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<StructureSection load='6hih' size='340' side='right'caption='[[6hih]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='6hih' size='340' side='right'caption='[[6hih]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6hih]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HIH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hih]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Metca Metca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HIH FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ccp, MCA2394 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243233 METCA])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6hih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hih OCA], [http://pdbe.org/6hih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hih RCSB], [http://www.ebi.ac.uk/pdbsum/6hih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hih ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6hih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hih OCA], [http://pdbe.org/6hih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hih RCSB], [http://www.ebi.ac.uk/pdbsum/6hih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hih ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nature is adept at utilising highly similar protein folds to carry out very different functions, yet the mechanisms by which this functional divergence occurs remain poorly characterised. In certain methanotrophic bacteria, two homologous pentacoordinate c-type heme proteins have been identified: a cytochrome P460 (cyt P460) and a cytochrome c'-beta (cyt cp-beta). Cytochromes P460 are able to convert hydroxylamine to nitrous oxide (N2O), a potent greenhouse gas. This reactivity is similar to that of hydroxylamine oxidoreductase (HAO), which is a key enzyme in nitrifying and methanotrophic bacteria. Cyt P460 and HAO both have unusual protein-heme cross-links, formed by a Tyr residue in HAO and a Lys in cyt P460. In contrast, cyts cp-beta (the only known cytochromes c' with a beta-sheet fold) lack this crosslink and appears to be optimized for binding non-polar molecules (including NO and CO) without enzymatic conversion. Our bioinformatics analysis supports the proposal that cyt cp-beta may have evolved from cyt P460 via a gene duplication event. Using high-resolution X-ray crystallography, UV-visible absorption, electron paramagnetic resonance (EPR) and resonance Raman spectroscopy, we have characterized the overall protein folding and active site structures of cyt cp-beta and cyt P460 from the obligate methanotroph, Methylococcus capsulatus (Bath). These proteins display a similar beta-sheet protein fold, together with a pattern of changes to the heme pocket regions and localised tertiary structure that have converted a hydroxylamine oxidizing enzyme into a gas-binding protein. Structural comparisons provide insights relevant to enzyme redesign for synthetic enzymology and engineering of gas sensor proteins. We also show the widespread occurrence of cyts cp-beta and characterise their phylogeny. | ||
| + | |||
| + | One fold, two functions: cytochrome P460 and cytochrome c'-beta from the methanotroph Methylococcus capsulatus (Bath).,Adams HR, Krewson C, Vardanega JE, Fujii S, Moreno T, Chicano, Sambongi Y, Svistunenko D, Paps J, Andrew CR, Hough MA Chem Sci. 2019 Jan 21;10(10):3031-3041. doi: 10.1039/c8sc05210g. eCollection 2019, Mar 14. PMID:30996884<ref>PMID:30996884</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6hih" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Metca]] | ||
[[Category: Adams, H]] | [[Category: Adams, H]] | ||
[[Category: Chicano, T M]] | [[Category: Chicano, T M]] | ||
Revision as of 09:14, 1 May 2019
Cytochrome c prime beta from Methylococcus capsulatus (Bath)
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Categories: Large Structures | Metca | Adams, H | Chicano, T M | Hough, M A | Co | Cytochrome | Methanotroph | No | Oxidoreductase
