5t26: Difference between revisions

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==Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor Acetopyruvate with Dihydrodipicolinate Synthase from Escherichia coli.==
==Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor Acetopyruvate with Dihydrodipicolinate Synthase from Escherichia coli.==
<StructureSection load='5t26' size='340' side='right' caption='[[5t26]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5t26' size='340' side='right'caption='[[5t26]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5t26]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T26 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5t26]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_IAI1 Escherichia coli IAI1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T26 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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]] 2.1&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=74P:(E)-N~6~-(1-CARBOXY-3-OXOBUTYLIDENE)-L-LYSINE'>74P</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=74P:(E)-N~6~-(1-CARBOXY-3-OXOBUTYLIDENE)-L-LYSINE'>74P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5t25|5t25]]</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=5t26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t26 OCA], [https://pdbe.org/5t26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t26 RCSB], [https://www.ebi.ac.uk/pdbsum/5t26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t26 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5t26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t26 OCA], [http://pdbe.org/5t26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t26 RCSB], [http://www.ebi.ac.uk/pdbsum/5t26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t26 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DAPA_ECO8A DAPA_ECO8A]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418]  
[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>
 
==See Also==
*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
[[Category: Escherichia coli IAI1]]
[[Category: Chooback, L]]
[[Category: Large Structures]]
[[Category: Fleming, C D]]
[[Category: Chooback L]]
[[Category: Karsten, W E]]
[[Category: Fleming CD]]
[[Category: Seabourn, P]]
[[Category: Karsten WE]]
[[Category: Thomas, L M]]
[[Category: Seabourn P]]
[[Category: Acetopyruvate modification]]
[[Category: Thomas LM]]
[[Category: Dihydrodipicolinate synthase]]
[[Category: Kinetic]]
[[Category: Lyase]]

Latest revision as of 15:53, 4 October 2023

Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor Acetopyruvate with Dihydrodipicolinate Synthase from Escherichia coli.Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor Acetopyruvate with Dihydrodipicolinate Synthase from Escherichia coli.

Structural highlights

5t26 is a 2 chain structure with sequence from Escherichia coli IAI1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
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

5t26, resolution 2.10Å

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