4fwy
From Proteopedia
(Difference between revisions)
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- | [[ | + | ==F33Y CuB myoglobin (F33Y L29H F43H sperm whale myoglobin) with copper bound== |
+ | <StructureSection load='4fwy' size='340' side='right' caption='[[4fwy]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4fwy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FWY FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fwx|4fwx]], [[4fwz|4fwz]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 Physeter catodon])</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=4fwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fwy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fwy RCSB], [http://www.ebi.ac.uk/pdbsum/4fwy PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | No spare Tyr: Rational design of functional enzymes with a high number of turnovers is a challenge, especially those with a complex active site, such as respiratory oxidases. Introducing two His and one Tyr residues into myoglobin resulted in enzymes that reduce O(2) to H(2) O with more than 1000 turnovers (red line, see scheme) and minimal release of reactive oxygen species. The positioning of the Tyr residue is critical for activity. | ||
- | + | A Designed Functional Metalloenzyme that Reduces O(2) to H(2) O with Over One Thousand Turnovers.,Miner KD, Mukherjee A, Gao YG, Null EL, Petrik ID, Zhao X, Yeung N, Robinson H, Lu Y Angew Chem Int Ed Engl. 2012 Jun 4;51(23):5589-92. doi: 10.1002/anie.201201981., Epub 2012 Apr 26. PMID:22539151<ref>PMID:22539151</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
- | + | ==See Also== | |
- | + | *[[Myoglobin|Myoglobin]] | |
- | == | + | == References == |
- | [[ | + | <references/> |
- | + | __TOC__ | |
- | == | + | </StructureSection> |
- | < | + | |
[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
- | [[Category: Gao, Y G | + | [[Category: Gao, Y G]] |
- | [[Category: Lu, Y | + | [[Category: Lu, Y]] |
- | [[Category: Miner, K D | + | [[Category: Miner, K D]] |
- | [[Category: Petrik, I D | + | [[Category: Petrik, I D]] |
- | [[Category: Robinson, H | + | [[Category: Robinson, H]] |
[[Category: Globin]] | [[Category: Globin]] | ||
[[Category: Oxidase]] | [[Category: Oxidase]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] |
Revision as of 21:06, 24 December 2014
F33Y CuB myoglobin (F33Y L29H F43H sperm whale myoglobin) with copper bound
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Categories: Physeter catodon | Gao, Y G | Lu, Y | Miner, K D | Petrik, I D | Robinson, H | Globin | Oxidase | Transport protein