PDBsum entry: 1bhz

Hydrolase

PDB id: 1bhz

Contents

Protein chain

129 a.a. *

* Residue conservation analysis

PDB id:

1bhz

Name:

Hydrolase

Title:

Low temperature middle resolution structure of hen egg white lysozyme from masc data

Structure:

Lysozyme. Chain: a. Ec: 3.2.1.17

Source:

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

Resolution:

3.90Å R-factor: 0.315 R-free: 0.308

Authors:

M.Ramin,W.Shepard,R.Fourme,R.Kahn

Key ref:

M.Ramin et al. (1999). Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values. Acta Crystallogr D Biol Crystallogr, 55, 157-167. PubMed id: 10089406 DOI: 10.1107/S090744499800626X

Date:

10-Jun-98 Release date: 04-Nov-98

Protein chain

P00698  (LYSC_CHICK) -  Lysozyme C

Seq: 147 a.a.

Struc: 129 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.17 - Lysozyme.
• 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 

• Cellular component: extracellular region (2 terms)
• Biological process: metabolic process (4 terms)
• Biochemical function: catalytic activity (5 terms)

DOI no: 10.1107/S090744499800626X

Acta Crystallogr D Biol Crystallogr 55:157-167 (1999)

PubMed id: 10089406

Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values.

M.Ramin, W.Shepard, R.Fourme, R.Kahn.

ABSTRACT

A previous article [Fourme et al. (1995). J. Synchrotron Rad. 2, 36-48] presented the theoretical foundations of MASC, a new contrast-variation method using multiwavelength anomalous scattering, and reported the first experimental results. New experiments have been conducted both at the ESRF (Grenoble, France) and at LURE-DCI (Orsay, France), using cryocooled crystals of three proteins of known structures and very different molecular weights. Amplitudes of ¿GammaT(h)¿, the 'normal' structure factors of the anomalously scattering part of the crystal including the solvent zone and the ordered anomalous scattering sites (if any), have been extracted from multiwavelength data. In the very low resolution range (d >/= 20 A), the agreement between experimental ¿GammaT(h)¿ and model values calculated from the bulk solvent is all the more satisfactory since the molecular weight of the protein is high. For spacings between 10 and 20 A, the agreement between experimental ¿GammaT(h)¿ and model values is also satisfactory if one takes into account ordered anomalous scatterer sites. Such sites have been found in the three cases.

Selected figure(s)

Figure 5.
Figure 5 Section z = 0 of the phased anomalous Fourier-difference map of P64k in 3.5 M (NH[4])[2]SeO[4] contoured at 3 above the mean density superimposed with an envelope model section of P64k at low temperature.

Figure 7.
Figure 7 Section z = 0.094 of the phased anomalous Fourier-difference map of HEWL in 0.5 M YbCl[3] contoured at 3 above the mean density superimposed with an envelope model section of HEWL at low temperature. The Yb atoms are located near the surface and/or in crevices.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 157-167) copyright 1999.

Figures were selected by an automated process.