2fyf: Difference between revisions

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<StructureSection load='2fyf' size='340' side='right'caption='[[2fyf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2fyf' size='340' side='right'caption='[[2fyf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fyf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FYF FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fyf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FYF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.5&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">serC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PC4:TETRACHLOROPLATINATE(II)'>PC4</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoserine_transaminase Phosphoserine transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.52 2.6.1.52] </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=2fyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyf OCA], [https://pdbe.org/2fyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fyf RCSB], [https://www.ebi.ac.uk/pdbsum/2fyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fyf 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=2fyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fyf OCA], [https://pdbe.org/2fyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fyf RCSB], [https://www.ebi.ac.uk/pdbsum/2fyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fyf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SERC_MYCTU SERC_MYCTU]] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine (By similarity).[HAMAP-Rule:MF_00160]  
[https://www.uniprot.org/uniprot/SERC_MYCTU SERC_MYCTU] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine (By similarity).[HAMAP-Rule:MF_00160]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fyf ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fyf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mycobacterium tuberculosis (Mtb), the causative agent of TB, remains a serious world health problem owing to limitations of the available drugs and the emergence of resistant strains. In this context, key biosynthetic enzymes from Mtb are attractive targets for the development of new therapeutic drugs. Here, the 1.5 A resolution crystal structure of Mtb phosphoserine aminotransferase (MtbPSAT) in complex with its cofactor, pyridoxal 5'-phosphate (PLP), is reported. MtbPSAT is an essential enzyme in the biosynthesis of serine and in pathways of one-carbon metabolism. The structure shows that although the Mtb enzyme differs substantially in sequence from other PSAT enzymes, its fold is conserved and its PLP-binding site is virtually identical. Structural comparisons suggest that this site remains unchanged throughout the catalytic cycle. On the other hand, PSAT enzymes are obligate dimers in which the two active sites are located in the dimer interface and distinct differences in the MtbPSAT dimer are noted. These impact on the substrate-binding region and access channel and suggest options for the development of selective inhibitors.
Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis.,Coulibaly F, Lassalle E, Baker HM, Baker EN Acta Crystallogr D Biol Crystallogr. 2012 May;68(Pt 5):553-63. Epub 2012 Apr 17. PMID:22525753<ref>PMID:22525753</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fyf" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Phosphoserine aminotransferase|Phosphoserine aminotransferase]]
*[[Phosphoserine aminotransferase|Phosphoserine aminotransferase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Myctu]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Phosphoserine transaminase]]
[[Category: Baker EN]]
[[Category: Baker, E N]]
[[Category: Coulibaly F]]
[[Category: Coulibaly, F]]
[[Category: Lassalle E]]
[[Category: Lassalle, E]]
[[Category: XMTB, Mycobacterium Tuberculosis Structural Proteomics Project]]
[[Category: Dimer]]
[[Category: Mycobacterium tuberculosis structural proteomics project]]
[[Category: Plp-dependent enzyme]]
[[Category: Structural genomic]]
[[Category: Transferase]]
[[Category: Xmtb]]

Latest revision as of 12:25, 14 February 2024

Structure of a putative phosphoserine aminotransferase from Mycobacterium TuberculosisStructure of a putative phosphoserine aminotransferase from Mycobacterium Tuberculosis

Structural highlights

2fyf is a 2 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SERC_MYCTU Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine (By similarity).[HAMAP-Rule:MF_00160]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2fyf, resolution 1.50Å

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