9iz5
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Multifunctional PLP-dependent enzyme TM1270== | |
| - | + | <StructureSection load='9iz5' size='340' side='right'caption='[[9iz5]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9iz5]] is a 2 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=9IZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9IZ5 FirstGlance]. <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]] 1.7Å</td></tr> | |
| - | [[Category: | + | <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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=9iz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9iz5 OCA], [https://pdbe.org/9iz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9iz5 RCSB], [https://www.ebi.ac.uk/pdbsum/9iz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9iz5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ALGLR_THEMA ALGLR_THEMA] Catalyzes the racemization of L-alanine to D-alanine, and of L-glutamate to D-glutamate. The activity is low, but likely physiological since T.maritima lacks canonical alr and murI genes, while D-alanine and D-glutamate are essential components of peptidoglycan. Also displays a more efficient cystathionine beta-lyase (CBL) activity, cleaving cystathionine to homocysteine and pyruvate; however, this reaction seems not to be physiologically relevant since T.maritima possesses an O-acetyl-homoserine thiolase (MetY) that bypasses the need of CBL for methionine biosynthesis. Is not able to produce cystathionine, using either O-acetylhomoserine or O-succinylhomoserine, plus L-cysteine as substrates, and thus does not possess cystathionine gamma-synthase (CGS) activity.<ref>PMID:28640457</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermotoga maritima MSB8]] | ||
| + | [[Category: Fushinobu S]] | ||
| + | [[Category: Miyamoto T]] | ||
| + | [[Category: Nitta S]] | ||
Current revision
Multifunctional PLP-dependent enzyme TM1270
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