From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2rsp.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2rsp.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2rsp| PDB=2rsp | SCENE= }} | | {{STRUCTURE_2rsp| PDB=2rsp | SCENE= }} |
| | | | |
| - | '''STRUCTURE OF THE ASPARTIC PROTEASE FROM ROUS SARCOMA RETROVIRUS REFINED AT 2 ANGSTROMS RESOLUTION'''
| + | ===STRUCTURE OF THE ASPARTIC PROTEASE FROM ROUS SARCOMA RETROVIRUS REFINED AT 2 ANGSTROMS RESOLUTION=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The structure of Rous sarcoma virus protease has been solved by multiple isomorphous replacement in the crystal form belonging to space group P3(1)21, with unit-cell parameters a = 88.95 A and c = 78.90 A. The enzyme belongs to the family of aspartic proteases with two identical subunits composing the active homodimer. The noncrystallographic dyad relating these two subunits was identified after preliminary tracing in the MIR map and was used for phase improvement by electron-density averaging. Structure refinement resulted in a model that included 1772 protein atoms and 252 water molecules, with an R factor of 0.144 for data extending to 2 A. The secondary structure of a retroviral protease molecule closely resembles that of a single domain in pepsin-like aspartic proteases and consists of several beta-strands and of one well-defined and one distorted alpha-helix. The dimer interface is composed of the N- and C-terminal chains from both subunits which are intertwined to form a well-ordered four-stranded antiparallel beta-sheet. In each monomer, the catalytic triad (Asp-Ser-Gly) is located in a loop that forms a part of the psi-structure characteristic to all aspartic proteases. The position of a water molecule between the active-site aspartate residues and the general scheme of H bonding within the active site bear close resemblance to those in pepsin-like aspartic proteases and therefore suggest a similar enzymatic mechanism. The binding cleft over the active site is covered by two flap arms, one from each monomer, which are partially disordered. The retroviral protease dimer has been compared with several enzymes of cellular origin, with chains aligning to an rms deviation of 1.90 A or better. | + | The line below this paragraph, {{ABSTRACT_PUBMED_2166563}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 2166563 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_2166563}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 25: |
Line 29: |
| | [[Category: Miller, M.]] | | [[Category: Miller, M.]] |
| | [[Category: Wlodawer, A.]] | | [[Category: Wlodawer, A.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:15:28 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:58:08 2008'' |
Revision as of 21:58, 28 July 2008
Template:STRUCTURE 2rsp
STRUCTURE OF THE ASPARTIC PROTEASE FROM ROUS SARCOMA RETROVIRUS REFINED AT 2 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 2166563
About this Structure
2RSP is a Single protein structure of sequence from Rous sarcoma virus. Full crystallographic information is available from OCA.
Reference
Structure of the aspartic protease from Rous sarcoma retrovirus refined at 2-A resolution., Jaskolski M, Miller M, Rao JK, Leis J, Wlodawer A, Biochemistry. 1990 Jun 26;29(25):5889-98. PMID:2166563
Page seeded by OCA on Tue Jul 29 00:58:08 2008
