This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1yxd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1yxd" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:1yxd.png|left|200px]]
 
- 
{{STRUCTURE_1yxd| PDB=1yxd | SCENE= }}
{{STRUCTURE_1yxd| PDB=1yxd | SCENE= }}
- 
===Structure of E. coli dihydrodipicolinate synthase bound with allosteric inhibitor (S)-lysine to 2.0 A===
===Structure of E. coli dihydrodipicolinate synthase bound with allosteric inhibitor (S)-lysine to 2.0 A===
 +
{{ABSTRACT_PUBMED_16041077}}
-
{{ABSTRACT_PUBMED_16041077}}
+
==Function==
 +
[[http://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>
==About this Structure==
==About this Structure==
Line 14: Line 13:
==Reference==
==Reference==
-
<ref group="xtra">PMID:016041077</ref><references group="xtra"/>
+
<ref group="xtra">PMID:016041077</ref><references group="xtra"/><references/>
-
[[Category: Dihydrodipicolinate synthase]]
+
[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Dobson, R C.J.]]
[[Category: Dobson, R C.J.]]

Revision as of 05:20, 28 August 2013

Template:STRUCTURE 1yxd

Contents

Structure of E. coli dihydrodipicolinate synthase bound with allosteric inhibitor (S)-lysine to 2.0 A

Template:ABSTRACT PUBMED 16041077

Function

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

About this Structure

1yxd is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

Reference

  • Dobson RC, Griffin MD, Jameson GB, Gerrard JA. The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance. Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1116-24. Epub 2005, Jul 20. PMID:16041077 doi:10.1107/S0907444905016318
  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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yxd"
Personal tools