4eou: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(One intermediate revision by the same user not shown)
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4eou]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ubs 3ubs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EOU FirstGlance]. <br>
<table><tr><td colspan='2'>[[4eou]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ubs 3ubs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EOU FirstGlance]. <br>
</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=LYF:(2E,4S)-2-{[(5S)-5-AMINO-5-CARBOXYPENTYL]IMINO}-4-HYDROXYHEPTANEDIOIC+ACID'>LYF</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]] 2.3&#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=LYF:(2E,4S)-2-{[(5S)-5-AMINO-5-CARBOXYPENTYL]IMINO}-4-HYDROXYHEPTANEDIOIC+ACID'>LYF</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=4eou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eou OCA], [https://pdbe.org/4eou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eou RCSB], [https://www.ebi.ac.uk/pdbsum/4eou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eou ProSAT]</span></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=4eou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eou OCA], [https://pdbe.org/4eou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eou RCSB], [https://www.ebi.ac.uk/pdbsum/4eou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eou ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of Escherichia coli dihydrodipicolinate synthase with pyruvate and substrate analogue succinic acid semi-aldehyde condensed with the active site lysine-161 was solved to a resolution of 2.3 A. Comparative analysis to a previously reported structure both resolves the configuration at the aldol addition centre, where the final addition product clearly displays the (S)-configuration, and the final conformation of the adduct within the active site. Direct comparison to two other crystal structures found in the Protein Data Bank, 1YXC and 3DU0, demonstrates significant similarity between the active site residues of these structures. Proteins 2012. (c) 2012 Wiley Periodicals, Inc.
 
The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semi-aldehyde: Unambiguous resolution of the stereochemistry of the condensation product.,Boughton BA, Dobson RC, Hutton CA Proteins. 2012 May 2. doi: 10.1002/prot.24106. PMID:22552955<ref>PMID:22552955</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4eou" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 15:06, 14 March 2024

Crystal structure of E. coli dihydrodipicolinate synthase with pyruvate and succinic semi-aldehyde bound in active site

4eou, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=4eou&oldid=4100375"