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PDBsum entry 1x60

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protein links
Hydrolase PDB id
1x60
Jmol
Contents
Protein chain
79 a.a. *
* Residue conservation analysis
PDB id:
1x60
Name: Hydrolase
Title: Solution structure of the peptidoglycan binding domain of b. Subtilis cell wall lytic enzyme cwlc
Structure: Sporulation-specific n-acetylmuramoyl-l-alanine amidase. Chain: a. Fragment: residues 1-79. Synonym: cell wall hydrolase, autolysin. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
NMR struc: 30 models
Authors: M.Mishima,T.Shida,K.Yabuki,K.Kato,J.Sekiguchi,C.Kojima
Key ref:
M.Mishima et al. (2005). Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR. Biochemistry, 44, 10153-10163. PubMed id: 16042392 DOI: 10.1021/bi050624n
Date:
17-May-05     Release date:   09-Aug-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q06320  (CWLC_BACSU) -  Sporulation-specific N-acetylmuramoyl-L-alanine amidase
Seq:
Struc:
255 a.a.
79 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.5.1.28  - N-acetylmuramoyl-L-alanine amidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain bacterial cell-wall glycopeptides.

 

 
DOI no: 10.1021/bi050624n Biochemistry 44:10153-10163 (2005)
PubMed id: 16042392  
 
 
Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
M.Mishima, T.Shida, K.Yabuki, K.Kato, J.Sekiguchi, C.Kojima.
 
  ABSTRACT  
 
Bacillus subtilis CwlC is a cell wall lytic N-acetylmuramoyl-l-alanine amidase that plays an important role in mother-cell lysis during sporulation. The enzyme consists of an N-terminal catalytic domain with C-terminal tandem repeats. The repeats [repeat 1 (residues 184-219) and repeat 2 (residues 220-255)] are termed CwlCr. We report on the solution structure of CwlCr as determined by multidimensional NMR, including the use of 36 (h3)J(NC)'-derived hydrogen bond restraints and 64 residual (1)D(NH) dipolar couplings. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure consisting of a betaalphabetabetaalphabeta-fold containing numerous contacts between the repeats. Hydrophobic residues important for structural integrity are conserved between the repeats, and are located symmetrically. We also present NMR analysis of the circularly permuted repeat mutant of CwlCr. Secondary structure content from the chemical shifts and hydrogen bonds derived from (h3)J(NC)' show that the mutant folds into a structure similar to that of the wild type, suggesting that the repeats are exchangeable. This implies that conserved hydrophobic residues are crucial for maintaining the folding of the repeats. While monitoring the chemical shift perturbations following the addition of digested soluble peptidoglycan fragments, we identified two peptidoglycan interaction sites of CwlCr at the edges of the protein symmetrically, and they are located approximately 28 A from each other.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19880599 S.J.Arends, K.Williams, R.J.Scott, S.Rolong, D.L.Popham, and D.S.Weiss (2010).
Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA.
  J Bacteriol, 192, 242-255.  
20497503 S.Poggio, C.N.Takacs, W.Vollmer, and C.Jacobs-Wagner (2010).
A protein critical for cell constriction in the Gram-negative bacterium Caulobacter crescentus localizes at the division site through its peptidoglycan-binding LysM domains.
  Mol Microbiol, 77, 74-89.  
20015680 T.C.Marlovits, and C.E.Stebbins (2010).
Type III secretion systems shape up as they ship out.
  Curr Opin Microbiol, 13, 47-52.  
19400794 A.Möll, and M.Thanbichler (2009).
FtsN-like proteins are conserved components of the cell division machinery in proteobacteria.
  Mol Microbiol, 72, 1037-1053.  
19854895 J.Lutkenhaus (2009).
FtsN--trigger for septation.
  J Bacteriol, 191, 7381-7382.  
19684127 M.A.Gerding, B.Liu, F.O.Bendezú, C.A.Hale, T.G.Bernhardt, and P.A.de Boer (2009).
Self-enhanced accumulation of FtsN at Division Sites and Roles for Other Proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction.
  J Bacteriol, 191, 7383-7401.  
19025570 Y.Yang, and C.Li (2009).
Transcription and genetic analyses of a putative N-acetylmuramyl-L-alanine amidase in Borrelia burgdorferi.
  FEMS Microbiol Lett, 290, 164-173.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.