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Hydrolase PDB id
1jfx
Jmol
Contents
Protein chain
217 a.a. *
Metals
_CL ×8
Waters ×398
* Residue conservation analysis
PDB id:
1jfx
Name: Hydrolase
Title: Crystal structure of the bacterial lysozyme from streptomyces coelicolor at 1.65 a resolution
Structure: 1,4-beta-n-acetylmuramidase m1. Chain: a. Synonym: beta-1,4-n,6-o-diacetylmuramidase. Engineered: yes
Source: Streptomyces coelicolor. Organism_taxid: 1902. Gene: cel. Expressed in: streptomyces coelicolor. Expression_system_taxid: 1902.
Resolution:
1.65Å     R-factor:   0.152     R-free:   0.185
Authors: A.Rau,T.Hogg,R.Marquardt,R.Hilgenfeld
Key ref:
A.Rau et al. (2001). A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 A resolution. J Biol Chem, 276, 31994-31999. PubMed id: 11427528 DOI: 10.1074/jbc.M102591200
Date:
22-Jun-01     Release date:   05-Sep-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P25310  (LYSM1_STRGL) -  Lysozyme M1
Seq:
Struc: 		294 a.a.
217 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.17  - Lysozyme.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   3 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
DOI no: 10.1074/jbc.M102591200 J Biol Chem 276:31994-31999 (2001)
PubMed id: 11427528  
 
 
A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 A resolution.
A.Rau, T.Hogg, R.Marquardt, R.Hilgenfeld.
 
  ABSTRACT  
 
Cellosyl is a bacterial muramidase from Streptomyces coelicolor. Similar to other lysozymes, the enzyme cleaves the beta-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine units, but it also exhibits a beta-1,4-N,6-O-diacetylmuramidase activity. The latter enables Cellosyl to degrade the cell walls of Staphylococcus aureus, which are not hydrolyzed by chicken-, goose-, or bacteriophage T4-type lysozymes. The enzymatic activity and amino acid sequence of Cellosyl group it with lysozymes of the Chalaropsis type, for which no detailed structural information has been available so far. The crystal structure of Cellosyl from S. coelicolor has been determined to a resolution of 1.65 A and refined to an R-factor of 15.2%. The enzyme is comprised of a single domain and possesses an unusual beta/alpha-barrel fold. The last strand, beta 8, of the (beta/alpha)(5)beta(3)-barrel is found to be antiparallel to strands beta 7 and beta 1. Asp-9, Asp-98, and Glu-100 are located at the active site. The structure of Cellosyl exhibits a new lysozyme fold and represents a new class of polysaccharide-hydrolyzing beta/alpha-barrels.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Stereographic ribbon presentation of the overall fold of Cellosyl. Graphics were prepared with Molscript (33) and Raster3D (34); top, side view of the barrel; bottom, view inside the barrel, rotated by 90° with respect to the top view. Helices are depicted in red, loops in green, the parallel -strands in blue, and the antiparallel -strand is highlighted in yellow. 		Figure 6.
Fig. 6. Topology diagram of Cellosyl (left) and enolase (right). The antiparallel -strand is shaded.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 31994-31999) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19244251 G.Minasov, S.Padavattan, L.Shuvalova, J.S.Brunzelle, D.J.Miller, A.Baslé, C.Massa, F.R.Collart, T.Schirmer, and W.F.Anderson (2009).
Crystal structures of YkuI and its complex with second messenger cyclic Di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains.
  J Biol Chem, 284, 13174-13184.
PDB codes: 2bas 2w27
19277643 V.Blättel, K.Wirth, H.Claus, B.Schlott, P.Pfeiffer, and H.König (2009).
A lytic enzyme cocktail from Streptomyces sp. B578 for the control of lactic and acetic acid bacteria in wine.
  Appl Microbiol Biotechnol, 83, 839-848.  
18427895 M.Chen, H.Liu, Y.Bai, Z.Zhang, J.Liu, and Y.Zhang (2008).
Homologous-restraint polymerase chain reaction: an efficient and rapid protocol to clone multiple homologous genes.
  Curr Microbiol, 57, 51-54.  
18266855 W.Vollmer, B.Joris, P.Charlier, and S.Foster (2008).
Bacterial peptidoglycan (murein) hydrolases.
  FEMS Microbiol Rev, 32, 259-286.  
15904486 S.Nakai, E.C.Li-Chan, and J.Dou (2005).
Pattern similarity study of functional sites in protein sequences: lysozymes and cystatins.
  BMC Biochem, 6, 9.  
  16233413 H.J.Seo, M.Kitaoka, K.Ohmiya, and K.Hayashi (2003).
Substrate specificity of the N,6-O-diacetylmuramidase from Streptomyces globisporus.
  J Biosci Bioeng, 95, 313-316.  
  12413546 A.Vasella, G.J.Davies, and M.Böhm (2002).
Glycosidase mechanisms.
  Curr Opin Chem Biol, 6, 619-629.  
12198311 B.Monterroso, A.Albert, M.Martínez-Ripoll, P.García, J.L.García, M.Menéndez, and J.A.Hermoso (2002).
Crystallization and preliminary X-ray diffraction studies of the complete modular endolysin from Cp-1, a phage infecting Streptococcus pneumoniae.
  Acta Crystallogr D Biol Crystallogr, 58, 1487-1489.  
11785761 Y.Bourne, and B.Henrissat (2001).
Glycoside hydrolases and glycosyltransferases: families and functional modules.
  Curr Opin Struct Biol, 11, 593-600.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.