3wg7: Difference between revisions
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==A 1.9 angstrom radiation damage free X-ray structure of large (420KDa) protein by femtosecond crystallography== | ==A 1.9 angstrom radiation damage free X-ray structure of large (420KDa) protein by femtosecond crystallography== | ||
<StructureSection load='3wg7' size='340' side='right' caption='[[3wg7]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3wg7' size='340' side='right' caption='[[3wg7]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_oxidase Cytochrome-c oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.9.3.1 1.9.3.1] </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=3wg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wg7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3wg7 PDBsum]</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=3wg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wg7 OCA], [http://pdbe.org/3wg7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wg7 RCSB], [http://www.ebi.ac.uk/pdbsum/3wg7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wg7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3wg7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome c oxidase|Cytochrome c oxidase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 01:11, 6 August 2016
A 1.9 angstrom radiation damage free X-ray structure of large (420KDa) protein by femtosecond crystallographyA 1.9 angstrom radiation damage free X-ray structure of large (420KDa) protein by femtosecond crystallography
Structural highlights
Function[COX5B_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [COX7B_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [COX3_BOVIN] Subunits I, II and III form the functional core of the enzyme complex. [CX6A2_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [COX6C_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [COX2_BOVIN] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1. [COX7C_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [CX6B1_BOVIN] Connects the two COX monomers into the physiological dimeric form. [COX1_BOVIN] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. [COX41_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [CX7A1_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [COX8B_BOVIN] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [COX5A_BOVIN] This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. Publication Abstract from PubMedWe report a method of femtosecond crystallography for solving radiation damage-free crystal structures of large proteins at sub-angstrom spatial resolution, using a large single crystal and the femtosecond pulses of an X-ray free-electron laser (XFEL). We demonstrated the performance of the method by determining a 1.9-A radiation damage-free structure of bovine cytochrome c oxidase, a large (420-kDa), highly radiation-sensitive membrane protein. Determination of damage-free crystal structure of an X-ray-sensitive protein using an XFEL.,Hirata K, Shinzawa-Itoh K, Yano N, Takemura S, Kato K, Hatanaka M, Muramoto K, Kawahara T, Tsukihara T, Yamashita E, Tono K, Ueno G, Hikima T, Murakami H, Inubushi Y, Yabashi M, Ishikawa T, Yamamoto M, Ogura T, Sugimoto H, Shen JR, Yoshikawa S, Ago H Nat Methods. 2014 May 11. doi: 10.1038/nmeth.2962. PMID:24813624[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Bos taurus
- Cytochrome-c oxidase
- Ago, H
- Hatanaka, M
- Hikima, T
- Hirata, K
- Inubushi, Y
- Ishikawa, T
- Kato, K
- Kawahara, T
- Murakami, H
- Muramoto, K
- Ogura, T
- Shen, J R
- Shinzawa-Itoh, K
- Sugimoto, H
- Takemura, S
- Tono, K
- Tsukihara, T
- Ueno, G
- Yabashi, M
- Yamamoto, M
- Yamashita, E
- Yano, N
- Yoshikawa, S
- Electron transport complex iv
- Iron
- Membrane
- Motif
- Oxidation-reduction
- Oxidoreductase
- Protein interaction domain