7jzc: Difference between revisions

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New page: '''Unreleased structure''' The entry 7jzc is ON HOLD Authors: Board, A.J., Dobson, R.C.J. Description: Dihydrodipicolinate synthase S48W mutant with lysine in the allosteric site, and ...
 
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'''Unreleased structure'''


The entry 7jzc is ON HOLD
==Dihydrodipicolinate synthase S48W mutant with lysine in the allosteric site, and pyruvate in the catalytic site==
<StructureSection load='7jzc' size='340' side='right'caption='[[7jzc]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7jzc]] 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=7JZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JZC 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]] 2.07&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></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=7jzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jzc OCA], [https://pdbe.org/7jzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jzc RCSB], [https://www.ebi.ac.uk/pdbsum/7jzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jzc 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 S48W mutant 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 S48W mutant with lysine in the allosteric site, and pyruvate in the catalytic siteDihydrodipicolinate synthase S48W mutant with lysine in the allosteric site, and pyruvate in the catalytic site

Structural highlights

7jzc 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 2.07Å
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

7jzc, resolution 2.07Å

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