4fwz: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==Aquoferric CuB myoglobin (L29H F43H sperm whale myoglobin)== | ||
<StructureSection load='4fwz' size='340' side='right' caption='[[4fwz]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fwz]] 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=4FWZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FWZ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]], [[4fwy|4fwy]]</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=4fwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fwz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fwz RCSB], [http://www.ebi.ac.uk/pdbsum/4fwz 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 10:54, 25 December 2014
Aquoferric CuB myoglobin (L29H F43H sperm whale myoglobin)
| ||||||||||||
