This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5f2n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:30, 6 March 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of mycobacterial fatty acid O-methyltransferase in complex with SAH and 3-hydroxy-decanoate.==
==Crystal structure of mycobacterial fatty acid O-methyltransferase in complex with SAH and 3-hydroxy-decanoate.==
-
<StructureSection load='5f2n' size='340' side='right' caption='[[5f2n]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+
<StructureSection load='5f2n' size='340' side='right'caption='[[5f2n]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5f2n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F2N FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5f2n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_marinum_M Mycobacterium marinum M]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F2N FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5UF:(3~{S})-3-OXIDANYLDECANOIC+ACID'>5UF</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5f2k|5f2k]], [[5f2o|5f2o]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5UF:(3~{S})-3-OXIDANYLDECANOIC+ACID'>5UF</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=5f2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f2n OCA], [http://pdbe.org/5f2n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f2n RCSB], [http://www.ebi.ac.uk/pdbsum/5f2n PDBsum]</span></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=5f2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f2n OCA], [https://pdbe.org/5f2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f2n RCSB], [https://www.ebi.ac.uk/pdbsum/5f2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f2n ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/B2HHT4_MYCMM B2HHT4_MYCMM]
-
Transesterification of fatty acids yields the essential component of biodiesel, but current processes are cost-prohibitive and generate waste. Recent efforts make use of biocatalysts that are effective in diverting products from primary metabolism to yield fatty acid methyl esters in bacteria. These biotransformations require the fatty acid O-methyltransferase (FAMT) from Mycobacterium marinum (MmFAMT). Although this activity was first reported in the literature in 1970, the FAMTs have yet to be biochemically characterized. Here, we describe several crystal structures of MmFAMT, which highlight an unexpected structural conservation with methyltransferases that are involved in plant natural product metabolism. The determinants for ligand recognition are analyzed by kinetic analysis of structure-based active-site variants. These studies reveal how an architectural fold employed in plant natural product biosynthesis is used in bacterial fatty acid O-methylation.
+
-
 
+
-
Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase: A Catalyst for the Enzymatic Production of Biodiesel.,Petronikolou N, Nair SK Chem Biol. 2015 Nov 19;22(11):1480-90. doi: 10.1016/j.chembiol.2015.09.011. Epub , 2015 Oct 29. PMID:26526103<ref>PMID:26526103</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5f2n" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Nair, S K]]
+
[[Category: Large Structures]]
-
[[Category: Petronikolou, N]]
+
[[Category: Mycobacterium marinum M]]
-
[[Category: 3-hydroxy-decanoate]]
+
[[Category: Nair SK]]
-
[[Category: Fatty acid methyltransferase]]
+
[[Category: Petronikolou N]]
-
[[Category: Methyltransferase]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of mycobacterial fatty acid O-methyltransferase in complex with SAH and 3-hydroxy-decanoate.

PDB ID 5f2n

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5f2n"
Personal tools