4a26: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:


==The crystal structure of Leishmania major N5,N10- methylenetetrahydrofolate dehydrogenase/cyclohydrolase==
==The crystal structure of Leishmania major N5,N10- methylenetetrahydrofolate dehydrogenase/cyclohydrolase==
<StructureSection load='4a26' size='340' side='right' caption='[[4a26]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='4a26' size='340' side='right'caption='[[4a26]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4a26]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leima Leima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A26 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4a26]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leima Leima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A26 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4a26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a26 OCA], [http://pdbe.org/4a26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a26 RCSB], [http://www.ebi.ac.uk/pdbsum/4a26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a26 ProSAT]</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=4a26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a26 OCA], [https://pdbe.org/4a26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a26 RCSB], [https://www.ebi.ac.uk/pdbsum/4a26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a26 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Line 20: Line 20:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Leima]]
[[Category: Leima]]
[[Category: Cameron, S]]
[[Category: Cameron, S]]

Revision as of 10:39, 18 August 2022

The crystal structure of Leishmania major N5,N10- methylenetetrahydrofolate dehydrogenase/cyclohydrolaseThe crystal structure of Leishmania major N5,N10- methylenetetrahydrofolate dehydrogenase/cyclohydrolase

Structural highlights

4a26 is a 2 chain structure with sequence from Leima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Three enzyme activities in the protozoan Leishmania major, namely N(5),N(10)-methylenetetrahydrofolate dehydrogenase/N(5),N(10)-methenyltetrahydrofolate cyclohydrolase (DHCH) and N(10)-formyltetrahydrofolate ligase (FTL) produce the essential intermediate N(10)-formyltetrahydrofolate. Although trypanosomatids possess at least one functional DHCH, the same is not true for FTL, which is absent in Trypanosoma brucei. Here, we present the 2.7A resolution crystal structure of the bifunctional apo-DHCH from L. major, which is a potential drug target. Sequence alignments show that the cytosolic enzymes found in trypanosomatids share a high level of identity of approximately 60%. Additionally, residues that interact and participate in catalysis in the human homologue are conserved amongst trypanosomatid sequences and this may complicate attempts to derive potent, parasite specific DHCH inhibitors.

The crystal structure of Leishmania major N(5),N(10)-methylenetetrahydrofolate dehydrogenase/cyclohydrolase and assessment of a potential drug target.,Eadsforth TC, Cameron S, Hunter WN Mol Biochem Parasitol. 2012 Feb;181(2):178-85. Epub 2011 Nov 15. PMID:22108435[1]

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

References

  1. Eadsforth TC, Cameron S, Hunter WN. The crystal structure of Leishmania major N(5),N(10)-methylenetetrahydrofolate dehydrogenase/cyclohydrolase and assessment of a potential drug target. Mol Biochem Parasitol. 2012 Feb;181(2):178-85. Epub 2011 Nov 15. PMID:22108435 doi:10.1016/j.molbiopara.2011.11.004

4a26, resolution 2.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA