7c11

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:48, 29 November 2023) (edit) (undo)
 
Line 1: Line 1:
==Formate--tetrahydrofolate ligase from Methylobacterium extorquens CM4 strain==
==Formate--tetrahydrofolate ligase from Methylobacterium extorquens CM4 strain==
-
<StructureSection load='7c11' size='340' side='right'caption='[[7c11]]' scene=''>
+
<StructureSection load='7c11' size='340' side='right'caption='[[7c11]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C11 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7C11 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[7c11]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylorubrum_extorquens_CM4 Methylorubrum extorquens CM4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C11 FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7c11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c11 OCA], [http://pdbe.org/7c11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7c11 RCSB], [http://www.ebi.ac.uk/pdbsum/7c11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7c11 ProSAT]</span></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]] 2.815&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=7c11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c11 OCA], [https://pdbe.org/7c11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c11 RCSB], [https://www.ebi.ac.uk/pdbsum/7c11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c11 ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FTHS_METC4 FTHS_METC4]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Methylobacterium extorquens is a methylotroph model organism that has the ability to assimilate formate using the tetrahydrofolate (THF) pathway. The formate-tetrahydrofolate ligase from M. extorquens (MeFtfL) is an enzyme involved in the THF pathway that catalyzes the conversion of formate, THF, and ATP into formyltetrahydrofolate and ADP. To investigate the biochemical properties of MeFtfL, we evaluated the metal usage and enzyme kinetics of the enzyme. MeFtfL uses the Mg ion for catalytic activity, but also has activity for Mn and Ca ions. The enzyme kinetics analysis revealed that Km value of farmate was much higher than THF and ATP, which shows that the ligation activity of MeFtfL is highly dependent on formation concentration. We also determined the crystal structure of MeFtfL at 2.8 A resolution. MeFtfL functions as a tetramer, and each monomer consists of three domains. The structural superposition of MeFtfL with FtfL from Moorella thermoacetica allowed us to predict the substrate binding site of the enzyme.
 +
 +
Biochemical properties and crystal structure of formate-tetrahydrofolate ligase from Methylobacterium extorquens CM4.,Kim S, Lee SH, Seo H, Kim KJ Biochem Biophys Res Commun. 2020 Jul 30;528(3):426-431. doi:, 10.1016/j.bbrc.2020.05.198. Epub 2020 Jun 4. PMID:32505353<ref>PMID:32505353</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 7c11" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
 +
[[Category: Methylorubrum extorquens CM4]]
[[Category: Kim K-J]]
[[Category: Kim K-J]]
[[Category: Kim S]]
[[Category: Kim S]]
[[Category: Lee S]]
[[Category: Lee S]]
[[Category: Seo H]]
[[Category: Seo H]]

Current revision

Formate--tetrahydrofolate ligase from Methylobacterium extorquens CM4 strain

PDB ID 7c11

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools