2a6n: Difference between revisions

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[[Image:2a6n.png|left|200px]]


{{STRUCTURE_2a6n|  PDB=2a6n  |  SCENE=  }}
==Dihydrodipicolinate synthase (E. coli)- mutant R138A==
 
<StructureSection load='2a6n' size='340' side='right'caption='[[2a6n]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
===Dihydrodipicolinate synthase (E. coli)- mutant R138A===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2a6n]] 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=2A6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A6N FirstGlance]. <br>
{{ABSTRACT_PUBMED_16185069}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#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></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6n OCA], [https://pdbe.org/2a6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a6n RCSB], [https://www.ebi.ac.uk/pdbsum/2a6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a6n ProSAT]</span></td></tr>
[[2a6n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A6N OCA].  
</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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/2a6n_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a6n ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Dihydrodipicolinate Synthase|Dihydrodipicolinate Synthase]]
*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:016185069</ref><references group="xtra"/>
__TOC__
[[Category: Dihydrodipicolinate synthase]]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Clifford, V R.]]
[[Category: Large Structures]]
[[Category: Devenish, S R.]]
[[Category: Clifford VR]]
[[Category: Dobson, R C.]]
[[Category: Devenish SR]]
[[Category: Gerrard, J A.]]
[[Category: Dobson RC]]
[[Category: Jameson, G B.]]
[[Category: Gerrard JA]]
[[Category: Pearce, F G.]]
[[Category: Jameson GB]]
[[Category: Turner, L A.]]
[[Category: Pearce FG]]
[[Category: Beta-alpha-barrel]]
[[Category: Turner LA]]
[[Category: Dihydrodipicolinate synthase]]
[[Category: Lyase]]

Latest revision as of 12:11, 14 February 2024

Dihydrodipicolinate synthase (E. coli)- mutant R138ADihydrodipicolinate synthase (E. coli)- mutant R138A

Structural highlights

2a6n 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 1.94Å
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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

2a6n, resolution 1.94Å

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