7jzg: Difference between revisions

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New page: '''Unreleased structure''' The entry 7jzg is ON HOLD Authors: Board, A.J., Dobson, R.C.J. Description: Dihydrodipicolinate synthase mutant S48F with lysine in the allosteric site and p...
 
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'''Unreleased structure'''


The entry 7jzg is ON HOLD
==Dihydrodipicolinate synthase mutant S48F with lysine in the allosteric site and pyruvate in the catalytic site==
<StructureSection load='7jzg' size='340' side='right'caption='[[7jzg]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7jzg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JZG 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]] 1.82&#8491;</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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</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=7jzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jzg OCA], [https://pdbe.org/7jzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jzg RCSB], [https://www.ebi.ac.uk/pdbsum/7jzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jzg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DAPA_ECOLI DAPA_ECOLI] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:20503968</ref> <ref>PMID:8993314</ref>


Authors: Board, A.J., Dobson, R.C.J.
==See Also==
 
*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
Description: Dihydrodipicolinate synthase mutant S48F with lysine in the allosteric site and pyruvate in the catalytic site
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Dobson, R.C.J]]
__TOC__
[[Category: Board, A.J]]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Board AJ]]
[[Category: Dobson RCJ]]

Latest revision as of 18:15, 18 October 2023

Dihydrodipicolinate synthase mutant S48F with lysine in the allosteric site and pyruvate in the catalytic siteDihydrodipicolinate synthase mutant S48F with lysine in the allosteric site and pyruvate in the catalytic site

Structural highlights

7jzg is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.82Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DAPA_ECOLI Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[1] [2]

See Also

References

  1. ↑ Devenish SR, Blunt JW, Gerrard JA. NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase. J Med Chem. 2010 Jun 24;53(12):4808-12. doi: 10.1021/jm100349s. PMID:20503968 doi:10.1021/jm100349s
  2. ↑ Blickling S, Renner C, Laber B, Pohlenz HD, Holak TA, Huber R. Reaction mechanism of Escherichia coli dihydrodipicolinate synthase investigated by X-ray crystallography and NMR spectroscopy. Biochemistry. 1997 Jan 7;36(1):24-33. PMID:8993314 doi:10.1021/bi962272d

7jzg, resolution 1.82Å

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