View source for 8sbb


==Cryo-EM structure of FtAlkB==
<StructureSection load='8sbb' size='340' side='right'caption='[[8sbb]], [[Resolution|resolution]] 3.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8sbb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fontimonas_thermophila Fontimonas thermophila] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SBB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.59&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D12:DODECANE'>D12</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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=8sbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sbb OCA], [https://pdbe.org/8sbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sbb RCSB], [https://www.ebi.ac.uk/pdbsum/8sbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sbb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1I2KHB9_9GAMM A0A1I2KHB9_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Alkanes are the most energy-rich form of carbon and are widely dispersed in the environment. Their transformation by microbes represents a key step in the global carbon cycle. Alkane monooxygenase (AlkB), a membrane-spanning metalloenzyme, converts straight chain alkanes to alcohols in the first step of the microbially-mediated degradation of alkanes, thereby playing a critical role in the global cycling of carbon and the bioremediation of oil. AlkB biodiversity is attributed to its ability to oxidize alkanes of various chain lengths, while individual AlkBs target a relatively narrow range. Mechanisms of substrate selectivity and catalytic activity remain elusive. Here we report the cryo-EM structure of AlkB, which provides a distinct architecture for membrane enzymes. Our structure and functional studies reveal an unexpected diiron center configuration and identify molecular determinants for substrate selectivity. These findings provide insight into the catalytic mechanism of AlkB and shed light on its function in alkane-degrading microorganisms.

Structure and mechanism of the alkane-oxidizing enzyme AlkB.,Guo X, Zhang J, Han L, Lee J, Williams SC, Forsberg A, Xu Y, Austin RN, Feng L Nat Commun. 2023 Apr 17;14(1):2180. doi: 10.1038/s41467-023-37869-z. PMID:37069165<ref>PMID:37069165</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8sbb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fontimonas thermophila]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Feng L]]
[[Category: Zhang J]]