5ioq

From Proteopedia

(Difference between revisions)

Revision as of 02:38, 13 July 2016

Flavin-dependent thymidylate synthase in complex with FAD and deoxyuridine

Structural highlights

5ioq is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	5ior, 5ios, 5iot
Activity:	Thymidylate synthase (FAD), with EC number 2.1.1.148
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[THYX_THEMA] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate.

Publication Abstract from PubMed

Many microorganisms use flavin-dependent thymidylate synthase (FDTS) to synthesize the essential nucleotide 2'-deoxythymidine 5'-monophosphate (dTMP) from 2'-deoxyuridine 5'-monophosphate (dUMP), 5,10-methylenetetrahydrofolate (CH2THF), and NADPH. FDTSs have a structure that is unrelated to the thymidylate synthase used by humans and a very different mechanism. Here we report nuclear magnetic resonance evidence that FDTS ionizes N3 of dUMP using an active-site arginine. The ionized form of dUMP is largely responsible for the changes in the flavin absorbance spectrum of FDTS upon dUMP binding. dUMP analogues also suggest that the phosphate of dUMP acts as the base that removes the proton from C5 of the dUMP-methylene intermediate in the FDTS-catalyzed reaction. These findings establish additional differences between the mechanisms of FDTS and human thymidylate synthase.

Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase.,Stull FW, Bernard SM, Sapra A, Smith JL, Zuiderweg ER, Palfey BA Biochemistry. 2016 Jun 14;55(23):3261-9. doi: 10.1021/acs.biochem.6b00510. Epub, 2016 Jun 2. PMID:27214228^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Stull FW, Bernard SM, Sapra A, Smith JL, Zuiderweg ER, Palfey BA. Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase. Biochemistry. 2016 Jun 14;55(23):3261-9. doi: 10.1021/acs.biochem.6b00510. Epub, 2016 Jun 2. PMID:27214228 doi:http://dx.doi.org/10.1021/acs.biochem.6b00510

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ioq"

@@ Line 7: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ior|5ior]], [[5ios|5ios]], [[5iot|5iot]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase_(FAD) Thymidylate synthase (FAD)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.148 2.1.1.148] </span></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=5ioq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ioq OCA], [http://pdbe.org/5ioq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ioq RCSB], [http://www.ebi.ac.uk/pdbsum/5ioq PDBsum]</span></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=5ioq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ioq OCA], [http://pdbe.org/5ioq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ioq RCSB], [http://www.ebi.ac.uk/pdbsum/5ioq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ioq ProSAT]</span></td></tr>
 </table>
 == Function ==

5ioq

From Proteopedia

Revision as of 02:38, 13 July 2016

Flavin-dependent thymidylate synthase in complex with FAD and deoxyuridine

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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