From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1lzy.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1lzy.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1lzy| PDB=1lzy | SCENE= }} | | {{STRUCTURE_1lzy| PDB=1lzy | SCENE= }} |
| | | | |
| - | '''X-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM'''
| + | ===X-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Monoclinic crystals of turkey egg lysozyme (TEL, E.C. 3.2.1.17) were obtained from 2.2 M ammonium sulfate solution at pH 4.2. They belong to space group P2(1) with unit-cell dimensions a = 38.07, b = 33.20, c = 46.12 A and beta = 110.1 degrees, and contain one molecule in the asymmetric unit (V(m) = 1.91 A(3) Da(-1)). The three-dimensional structure of TEL was solved by the method of multiple isomorphous replacement with anomalous scattering. Area detector data to 1.5 A resolution from native and heavy-atom derivatives were used for the structure determination. The structure was refined by the simulated-annealing method with diffraction data of 10-1.30 A resolution. The conventional R factor was 0.189. The root-mean-square deviations from ideal bond distances and angles were 0.016 A and 2.9 degrees, respectively. The backbone structure of TEL is very similar to that of hen egg lysozyme (HEL) and the difference in seven amino-acid residues does not affect the basic folding of the polypeptide chain. Except for the region from Gly101 to Gly104, the geometry of the active-site cleft is conserved between TEL and HEL. The Gly101 residue is located at the end of the sugar-binding site and the structural change in this region between TEL and HEL is considered to be responsible for the difference in their enzymatic properties.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15299509}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15299509 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15299509}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 23: |
Line 27: |
| | [[Category: Single protein]] | | [[Category: Single protein]] |
| | [[Category: Harata, K.]] | | [[Category: Harata, K.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:27:58 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:54:28 2008'' |
Revision as of 19:54, 2 July 2008
Template:STRUCTURE 1lzy
X-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM
Template:ABSTRACT PUBMED 15299509
About this Structure
1LZY is a Single protein structure. Full crystallographic information is available from OCA.
Reference
X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution., Harata K, Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):497-504. PMID:15299509
Page seeded by OCA on Wed Jul 2 22:54:28 2008
