4air: Difference between revisions

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==Leishmania major cysteine synthase==
==Leishmania major cysteine synthase==
<StructureSection load='4air' size='340' side='right' caption='[[4air]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='4air' size='340' side='right'caption='[[4air]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4air]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AIR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AIR FirstGlance]. <br>
<table><tr><td colspan='2'>[[4air]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major] 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=4AIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AIR FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FGA:GAMMA-D-GLUTAMIC+ACID'>FGA</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] </span></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>, <scene name='pdbligand=FGA:GAMMA-D-GLUTAMIC+ACID'>FGA</scene></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4air FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4air OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4air RCSB], [http://www.ebi.ac.uk/pdbsum/4air 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=4air FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4air OCA], [https://pdbe.org/4air PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4air RCSB], [https://www.ebi.ac.uk/pdbsum/4air PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4air ProSAT]</span></td></tr>
<table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q4Q159_LEIMA Q4Q159_LEIMA]
Cysteine biosynthesis is a potential target for drug development against parasitic Leishmania species; these protozoa are responsible for a range of serious diseases. To improve understanding of this aspect of Leishmania biology, a crystallographic and biochemical study of L. major cysteine synthase has been undertaken, seeking to understand its structure, enzyme activity and modes of inhibition. Active enzyme was purified, assayed and crystallized in an orthorhombic form with a dimer in the asymmetric unit. Diffraction data extending to 1.8 A resolution were measured and the structure was solved by molecular replacement. A fragment of gamma-poly-D-glutamic acid, a constituent of the crystallization mixture, was bound in the enzyme active site. Although a D-glutamate tetrapeptide had insignificant inhibitory activity, the enzyme was competitively inhibited (K(i) = 4 microM) by DYVI, a peptide based on the C-terminus of the partner serine acetyltransferase with which the enzyme forms a complex. The structure surprisingly revealed that the cofactor pyridoxal phosphate had been lost during crystallization.
 
Structure of Leishmania major cysteine synthase.,Fyfe PK, Westrop GD, Ramos T, Muller S, Coombs GH, Hunter WN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):738-43., Epub 2012 Jun 22. PMID:22750854<ref>PMID:22750854</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cysteine synthase]]
[[Category: Large Structures]]
[[Category: Leishmania major]]
[[Category: Leishmania major]]
[[Category: Coombs, G H.]]
[[Category: Synthetic construct]]
[[Category: Fyfe, P K.]]
[[Category: Coombs GH]]
[[Category: Hunter, W N.]]
[[Category: Fyfe PK]]
[[Category: Westrop, G D.]]
[[Category: Hunter WN]]
[[Category: Transferase]]
[[Category: Westrop GD]]

Latest revision as of 10:47, 7 February 2024

Leishmania major cysteine synthaseLeishmania major cysteine synthase

Structural highlights

4air is a 4 chain structure with sequence from Leishmania major and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q4Q159_LEIMA

4air, resolution 1.80Å

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OCA
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