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Hydrolase PDB-id
1b2k
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Protein chains
129 a.a. *
Metal ions
IOD ×17
Waters ×291

* Residue conservation analysis
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PDB id: 1b2k
Name: Hydrolase
Title: Structural effects of monovalent anions on polymorphic lysozyme crystals

Structure:
Protein (lysozyme). Chain: a, b. Synonym: hen (gallus gallus) egg-white lysozyme, mucopeptide,n-acetylmuramyl hydrolase. Ec: 3.2.1.17

Source:
Gallus gallus. Chicken. Organism_taxid: 9031. Tissue: egg white. Cellular_location: cytoplasm (white)

UniProt:
Chains A, B: P00698 (LYSC_CHICK)
Pfam   ArchSchema ?
Seq: 147 a.a.
Struc: 129 a.a.
Key:    PfamA domain
 Secondary structure  CATH domain

Enzyme class:
E.C.3.2.1.17   [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.

Resolution:
1.60Å

R-factor:
0.198

R-free:
0.237

Authors:
M.C.Vaney,I.Broutin,M.Ries-Kautt,A.Ducruix

Key ref:
M.C.Vaney et al. (2001). Structural effects of monovalent anions on polymorphic lysozyme crystals.. Acta Crystallogr D Biol Crystallogr, 57, 929-940. [PubMed id: 11418760] [DOI: 10.1107/S0907444901004504]

Date:
26-Nov-98

Release date:
02-Dec-98
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    Key reference    
 
 
DOI no: 10.1107/S0907444901004504 Acta Crystallogr D Biol Crystallogr 57:929-940 (2001)
PubMed id: 11418760  
 
 
Structural effects of monovalent anions on polymorphic lysozyme crystals.
M.C.Vaney, I.Broutin, P.Retailleau, A.Douangamath, S.Lafont, C.Hamiaux, T.Prangé, A.Ducruix, M.Riès-Kautt.
 
  ABSTRACT  
 
Understanding direct salt effects on protein crystal polymorphism is addressed by comparing different crystal forms (triclinic, monoclinic, tetragonal and orthorhombic) for hen, turkey, bob white quail and human lysozymes. Four new structures of hen egg-white lysozyme are reported: crystals grown in the presence of NapTS diffracted to 1.85 A, of NaI to 1.6 A, of NaNO(3) to 1.45 A and of KSCN to 1.63 A. These new structures are compared with previously published structures in order to draw a mapping of the surface of different lysozymes interacting with monovalent anions, such as nitrate, chloride, iodide, bromide and thiocyanate. An analysis of the structural sites of these anions in the various lysozyme structures is presented. This study shows common anion sites whatever the crystal form and the chemical nature of anions, while others seem specific to a given geometry and a particular charge environment induced by the crystal packing.
 
  Selected figure(s)  
 
Figure 4.
Figure 4 R.m.s. deviations versus the sequence number between the two independent molecules of the HEWL/NaI monoclinic structure showing the non-equivalence of loops 65-75.
Figure 6.
Figure 6 All anionic sites (red numbers) aligned on the lysozyme sequence. The unique sites are labelled according to the chemical formula of the anion taken from the corresponding PDB file.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 929-940) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19706429 Y.Zhang, and P.S.Cremer (2009).
The inverse and direct Hofmeister series for lysozyme.
  Proc Natl Acad Sci U S A, 106, 15249-15253.  
17641629 M.Benvenuti, and S.Mangani (2007).
Crystallization of soluble proteins in vapor diffusion for x-ray crystallography.
  Nat Protoc, 2, 1633-1651.  
12684536 P.E.Mason, G.W.Neilson, C.E.Dempsey, A.C.Barnes, and J.M.Cruickshank (2003).
The hydration structure of guanidinium and thiocyanate ions: implications for protein stability in aqueous solution.
  Proc Natl Acad Sci U S A, 100, 4557-4561.  
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.