D-alanine-D-alanine ligase

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Function

D-alanine-D-alanine ligase (DDL) catalyzes the conversion of 2 alanine molecules and ATP to D-alanine-D-alanine and ADP. DDL is part of the bacterial peptidoglycan synthesis pathway and the alanine metabolism.[1]

Relevance

DDL acts in bacterial cell wall synthesis and its inhibition is a target of novel antibiotics search.

Structural highlights

DDL structure contains (Alpha Helices, Beta Strands , Loops , Turns). The is found between domains 1 and 2.[2]

3D structures of D-alanine-D-alanine ligase

D-alanine-D-alanine ligase 3D structures


Structure of D-alanine-D-alanine ligase dimer complex with ADP (stick model), sulfate and Mg+2 ion (green) (PDB entry 2i8c)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Fan C, Moews PC, Walsh CT, Knox JR. Vancomycin resistance: structure of D-alanine:D-alanine ligase at 2.3 A resolution. Science. 1994 Oct 21;266(5184):439-43. PMID:7939684
  2. ↑ Liu S, Chang JS, Herberg JT, Horng MM, Tomich PK, Lin AH, Marotti KR. Allosteric inhibition of Staphylococcus aureus D-alanine:D-alanine ligase revealed by crystallographic studies. Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15178-83. Epub 2006 Oct 2. PMID:17015835

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Michal Harel, Alexander Berchansky
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