From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1lmn.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1lmn.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1lmn| PDB=1lmn | SCENE= }} | | {{STRUCTURE_1lmn| PDB=1lmn | SCENE= }} |
| | | | |
| - | '''THE REFINED CRYSTAL STRUCTURE OF LYSOZYME FROM THE RAINBOW TROUT (ONCORHYNCHUS MYKISS)'''
| + | ===THE REFINED CRYSTAL STRUCTURE OF LYSOZYME FROM THE RAINBOW TROUT (ONCORHYNCHUS MYKISS)=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Lysozymes (E.C. 3.2.1.17) are well characterized ubiquitous enzymes that have an antibacterial effect. The lysozymes from rainbow trout (RBTL) (Oncorhynchus mykiss) could be particularly interesting in aquaculture since they show higher activity than egg-white lysozyme and lysozymes from other fish species against a variety of pathogenic bacteria. Two lysozymes, I and II, differing only in a single amino acid, were purified from the kidney of rainbow trout and shown to belong to the c-type class of lysozymes. The type II form was shown to be much more potent against a variety of bacteria than the type I enzyme. We have grown crystals from a mixture containing about 80% type I and 20% type II lysozyme from rainbow trout, and solved the X-ray crystal structure. The crystals are trigonal with a = 76.68, c = 54.46 A and space group P3(1)21. The phase problem was solved by the molecular-replacement method, and the structure was refined to an R-factor of 17.4% using data to 1.8 A resolution. The crystal structure shows that the three-dimensional structure of rainbow trout lysozyme is very similar to the previously solved structures of other c-type lysozymes. The single polypeptide of 129 amino acids is folded into two domains separated by a deep cleft which contains the active site. Secondary-structure elements, four alpha-helices and a three-stranded beta-sheet, are located in the same sequential positions as in the hen, turkey and human enzymes. The beta-sheet is found to be common for structures of both c- and g-type lysozymes. We suggest that differences in antibiotic activity of the two forms of RBTL are probably due to small differences in the hydophobicity of a small surface region.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15299303}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15299303 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15299303}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 25: |
Line 29: |
| | [[Category: Hough, E.]] | | [[Category: Hough, E.]] |
| | [[Category: Karlsen, S.]] | | [[Category: Karlsen, S.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:04:14 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:26:12 2008'' |
Revision as of 18:26, 2 July 2008
Template:STRUCTURE 1lmn
THE REFINED CRYSTAL STRUCTURE OF LYSOZYME FROM THE RAINBOW TROUT (ONCORHYNCHUS MYKISS)
Template:ABSTRACT PUBMED 15299303
About this Structure
1LMN is a Single protein structure of sequence from Oncorhynchus mykiss. Full crystallographic information is available from OCA.
Reference
Refined crystal structure of lysozyme from the rainbow trout (Oncorhynchus mykiss)., Karlsen S, Eliassen BE, Hansen LK, Larsen RL, Riise BW, Smalas AO, Hough E, Grinde B, Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):354-67. PMID:15299303
Page seeded by OCA on Wed Jul 2 21:26:12 2008
