From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1thm.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1thm.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1thm| PDB=1thm | SCENE= }} | | {{STRUCTURE_1thm| PDB=1thm | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF THERMITASE AT 1.4 ANGSTROMS RESOLUTION'''
| + | ===CRYSTAL STRUCTURE OF THERMITASE AT 1.4 ANGSTROMS RESOLUTION=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The crystal structure of thermitase, a subtilisin-type serine proteinase from Thermoactinomyces vulgaris, was determined by X-ray diffraction at 1.4 A resolution. The structure was solved by a combination of molecular and isomorphous replacement. The starting model was that of subtilisin BPN' from the Protein Data Bank, determined at 2.5 A resolution. The high-resolution refinement was based on data collected using synchrotron radiation with a Fuji image plate as detector. The model of thermitase refined to a conventional R factor of 14.9% and contains 1997 protein atoms, 182 water molecules and two Ca ions. The tertiary structure of thermitase is similar to that of the other subtilisins although there are some significant differences in detail. Comparison with subtilisin BPN' revealed two major structural differences. The N-terminal region in thermitase, which is absent in subtilisin BPN', forms a number of contacts with the tight Ca2+ binding site and indeed provides the very tight binding of the Ca ion. In thermitase the loop of residues 60 to 65 forms an additional (10) beta-strand of the central beta-sheet and the second Ca2+ binding site that has no equivalent in the subtilisin BPN' structure. The observed differences in the Ca2+ binding and the increased number of ionic and aromatic interactions in thermitase are likely sources of the enhanced stability of thermitase. | + | The line below this paragraph, {{ABSTRACT_PUBMED_2196375}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 2196375 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_2196375}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 26: |
Line 30: |
| | [[Category: Kuranova, I P.]] | | [[Category: Kuranova, I P.]] |
| | [[Category: Teplyakov, A V.]] | | [[Category: Teplyakov, A V.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:57:25 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:05:40 2008'' |
Revision as of 12:05, 29 July 2008
Template:STRUCTURE 1thm
CRYSTAL STRUCTURE OF THERMITASE AT 1.4 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 2196375
About this Structure
1THM is a Single protein structure of sequence from Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.
Reference
Crystal structure of thermitase at 1.4 A resolution., Teplyakov AV, Kuranova IP, Harutyunyan EH, Vainshtein BK, Frommel C, Hohne WE, Wilson KS, J Mol Biol. 1990 Jul 5;214(1):261-79. PMID:2196375
Page seeded by OCA on Tue Jul 29 15:05:40 2008
