PDBsum entry 2eql

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protein links
Hydrolase(o-glycosyl) PDB id
Protein chain
129 a.a. *
* Residue conservation analysis
PDB id:
Name: Hydrolase(o-glycosyl)
Title: Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 angstroms resolution
Structure: Horse milk lysozyme. Chain: a. Engineered: yes
Source: Equus caballus. Horse. Organism_taxid: 9796
2.50Å     R-factor:   0.234    
Authors: H.Tsuge,H.Ago,M.Miyano
Key ref: H.Tsuge et al. (1992). Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution. J Biochem, 111, 141-143. PubMed id: 1569037
27-May-94     Release date:   31-Jul-94    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P11376  (LYSC1_HORSE) -  Lysozyme C, milk isozyme
129 a.a.
129 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - 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     metabolic process   3 terms 
  Biochemical function     catalytic activity     5 terms  


J Biochem 111:141-143 (1992)
PubMed id: 1569037  
Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution.
H.Tsuge, H.Ago, M.Noma, K.Nitta, S.Sugai, M.Miyano.
The crystal structure of a calcium binding equine lysozyme has been determined at 2.5 A resolution by means of molecular replacement. The energy minimized equine lysozyme as the starting model, was refined with the molecular dynamics program, X-PLOR, and the R factor of the current model was found to be 24% without any water molecules. The conformation of the calcium binding loop is similar to that of alpha-lactalbumin. The profiles of backbone atomic displacements throughout the lysozyme and alpha-lactalbumin superfamilies are comparable as well as their homologous tertiary structures.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19594832 K.Wilhelm, A.Darinskas, W.Noppe, E.Duchardt, K.H.Mok, V.Vukojević, J.Schleucher, and L.A.Morozova-Roche (2009).
Protein oligomerization induced by oleic acid at the solid-liquid interface--equine lysozyme cytotoxic complexes.
  FEBS J, 276, 3975-3989.  
19651623 V.Casaite, S.Bruzyte, V.Bukauskas, A.Setkus, L.A.Morozova-Roche, and R.Meskys (2009).
Expression and purification of active recombinant equine lysozyme in Escherichia coli.
  Protein Eng Des Sel, 22, 649-654.  
12211019 M.Mizuguchi, Y.Kobashigawa, Y.Kumaki, M.Demura, K.Kawano, and K.Nitta (2002).
Effects of a helix substitution on the folding mechanism of bovine alpha-lactalbumin.
  Proteins, 49, 95.  
10861388 E.W.Blanch, L.A.Morozova-Roche, L.Hecht, W.Noppe, and L.D.Barron (2000).
Raman optical activity characterization of native and molten globule states of equine lysozyme: comparison with hen lysozyme and bovine alpha-lactalbumin.
  Biopolymers, 57, 235-248.  
10727216 T.Koshiba, M.Yao, Y.Kobashigawa, M.Demura, A.Nakagawa, I.Tanaka, K.Kuwajima, and K.Nitta (2000).
Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme.
  Biochemistry, 39, 3248-3257.
PDB code: 1qqy
  9385633 A.C.Wallace, N.Borkakoti, and J.M.Thornton (1997).
TESS: a geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites.
  Protein Sci, 6, 2308-2323.  
  9307874 P.K.Qasba, and S.Kumar (1997).
Molecular divergence of lysozymes and alpha-lactalbumin.
  Crit Rev Biochem Mol Biol, 32, 255-306.  
7552711 L.A.Morozova, D.T.Haynie, C.Arico-Muendel, H.Van Dael, and C.M.Dobson (1995).
Structural basis of the stability of a lysozyme molten globule.
  Nat Struct Biol, 2, 871-875.  
7832986 K.R.Acharya, D.I.Stuart, D.C.Phillips, H.A.McKenzie, and C.G.Teahan (1994).
Models of the three-dimensional structures of echidna, horse, and pigeon lysozymes: calcium-binding lysozymes and their relationship with alpha-lactalbumins.
  J Protein Chem, 13, 569-584.  
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