View source for 3zom


==M.acetivorans protoglobin F145W mutant==
<StructureSection load='3zom' size='340' side='right'caption='[[3zom]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zom]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans Methanosarcina acetivorans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZOM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZOM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3zom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zom OCA], [https://pdbe.org/3zom PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zom RCSB], [https://www.ebi.ac.uk/pdbsum/3zom PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zom ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8TLY9_METAC Q8TLY9_METAC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb*, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb*. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb*. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb* and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity.

Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans.,Tilleman L, Abbruzzetti S, Ciaccio C, De Sanctis G, Nardini M, Pesce A, Desmet F, Moens L, Van Doorslaer S, Bruno S, Bolognesi M, Ascenzi P, Coletta M, Viappiani C, Dewilde S PLoS One. 2015 Jun 5;10(6):e0125959. doi: 10.1371/journal.pone.0125959., eCollection 2015. PMID:26047471<ref>PMID:26047471</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zom" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanosarcina acetivorans]]
[[Category: Abbruzzetti S]]
[[Category: Ascenzi P]]
[[Category: Bolognesi M]]
[[Category: Bruno S]]
[[Category: Ciaccio C]]
[[Category: Coletta M]]
[[Category: De Sanctis G]]
[[Category: Desmet F]]
[[Category: Dewilde S]]
[[Category: Moens L]]
[[Category: Nardini M]]
[[Category: Pesce A]]
[[Category: Tilleman L]]
[[Category: Van Doorslaer S]]
[[Category: Viappiani C]]