7kb0: Difference between revisions

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'''Unreleased structure'''


The entry 7kb0 is ON HOLD  until Paper Publication
==O-acety-L-homoserine aminocarboxypropyltransferase (MetY) from Thermotoga maritima with pyridoxal-5-phosphate (PLP) bound in the internal aldimine state==
 
<StructureSection load='7kb0' size='340' side='right'caption='[[7kb0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
Authors: Brewster, J.L., Pachl, P., Squire, C., Selmer, M., Patrick, W.M.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[7kb0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KB0 FirstGlance]. <br>
Description: O-acety-L-homoserine aminocarboxypropyltransferase (MetY) from Thermotoga maritima with pyridoxal-5-phosphate (PLP) bound in the internal aldimine state
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
[[Category: Patrick, W.M]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7kb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kb0 OCA], [https://pdbe.org/7kb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kb0 RCSB], [https://www.ebi.ac.uk/pdbsum/7kb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kb0 ProSAT]</span></td></tr>
[[Category: Selmer, M]]
</table>
[[Category: Squire, C]]
== Function ==
[[Category: Brewster, J.L]]
[https://www.uniprot.org/uniprot/METY_THEMA METY_THEMA] Catalyzes the production of homocysteine from O-acetylhomoserine (OAH) and hydrogen sulfide (H2S), a step in the methionine biosynthesis pathway. Is not able to form cystathionine from O-acetylhomoserine and L-cysteine.<ref>PMID:28640457</ref>
[[Category: Pachl, P]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Brewster JL]]
[[Category: Pachl P]]
[[Category: Patrick WM]]
[[Category: Selmer M]]
[[Category: Squire C]]

Latest revision as of 10:17, 3 April 2024

O-acety-L-homoserine aminocarboxypropyltransferase (MetY) from Thermotoga maritima with pyridoxal-5-phosphate (PLP) bound in the internal aldimine stateO-acety-L-homoserine aminocarboxypropyltransferase (MetY) from Thermotoga maritima with pyridoxal-5-phosphate (PLP) bound in the internal aldimine state

Structural highlights

7kb0 is a 1 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

METY_THEMA Catalyzes the production of homocysteine from O-acetylhomoserine (OAH) and hydrogen sulfide (H2S), a step in the methionine biosynthesis pathway. Is not able to form cystathionine from O-acetylhomoserine and L-cysteine.[1]

References

  1. ↑ Ferla MP, Brewster JL, Hall KR, Evans GB, Patrick WM. Primordial-like enzymes from bacteria with reduced genomes. Mol Microbiol. 2017 Aug;105(4):508-524. doi: 10.1111/mmi.13737. Epub 2017 Jul 6. PMID:28640457 doi:http://dx.doi.org/10.1111/mmi.13737

7kb0, resolution 1.85Å

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