1fmb
From Proteopedia
(New page: 200px<br /> <applet load="1fmb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fmb, resolution 1.8Å" /> '''EIAV PROTEASE COMPLE...) |
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| - | [[Image:1fmb.gif|left|200px]]<br /> | + | [[Image:1fmb.gif|left|200px]]<br /><applet load="1fmb" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1fmb" size=" | + | |
caption="1fmb, resolution 1.8Å" /> | caption="1fmb, resolution 1.8Å" /> | ||
'''EIAV PROTEASE COMPLEXED WITH THE INHIBITOR HBY-793'''<br /> | '''EIAV PROTEASE COMPLEXED WITH THE INHIBITOR HBY-793'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Equine infectious anemia virus (EIAV), the causative agent of infectious | + | Equine infectious anemia virus (EIAV), the causative agent of infectious anemia in horses, is a member of the lentiviral family. The virus-encoded proteinase (PR) processes viral polyproteins into functional molecules during replication and it also cleaves viral nucleocapsid protein during infection. The X-ray structure of a complex of the 154G mutant of EIAV PR with the inhibitor HBY-793 was solved at 1.8 A resolution and refined to a crystallographic R-factor of 0.136. The molecule is a dimer in which the monomers are related by a crystallographic twofold axis. Although both the enzyme and the inhibitor are symmetric, the interactions between the central part of the inhibitor and the active site aspartates are asymmetric, and the inhibitor and the two flaps are partially disordered. The overall fold of EIAV PR is very similar to that of other retroviral proteinases. However, a novel feature of the EIAV PR structure is the appearance of the second alpha-helix in the monomer in a position predicted by the structural template for the family of aspartic proteinases. The parts of the EIAV PR with the highest resemblance to human immunodeficiency virus type 1 PR include the substrate-binding sites; thus, the differences in the specificity of both enzymes have to be explained by enzyme-ligand interactions at the periphery of the active site as well. |
==About this Structure== | ==About this Structure== | ||
| - | 1FMB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus] with HYB as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] Full crystallographic information is available from [http:// | + | 1FMB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus] with <scene name='pdbligand=HYB:'>HYB</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rna-directed dna polymerase]] | [[Category: rna-directed dna polymerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:10 2008'' |
Revision as of 10:40, 21 February 2008
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EIAV PROTEASE COMPLEXED WITH THE INHIBITOR HBY-793
Overview
Equine infectious anemia virus (EIAV), the causative agent of infectious anemia in horses, is a member of the lentiviral family. The virus-encoded proteinase (PR) processes viral polyproteins into functional molecules during replication and it also cleaves viral nucleocapsid protein during infection. The X-ray structure of a complex of the 154G mutant of EIAV PR with the inhibitor HBY-793 was solved at 1.8 A resolution and refined to a crystallographic R-factor of 0.136. The molecule is a dimer in which the monomers are related by a crystallographic twofold axis. Although both the enzyme and the inhibitor are symmetric, the interactions between the central part of the inhibitor and the active site aspartates are asymmetric, and the inhibitor and the two flaps are partially disordered. The overall fold of EIAV PR is very similar to that of other retroviral proteinases. However, a novel feature of the EIAV PR structure is the appearance of the second alpha-helix in the monomer in a position predicted by the structural template for the family of aspartic proteinases. The parts of the EIAV PR with the highest resemblance to human immunodeficiency virus type 1 PR include the substrate-binding sites; thus, the differences in the specificity of both enzymes have to be explained by enzyme-ligand interactions at the periphery of the active site as well.
About this Structure
1FMB is a Single protein structure of sequence from Equine infectious anemia virus with as ligand. Active as HIV-1 retropepsin, with EC number 3.4.23.16 Full crystallographic information is available from OCA.
Reference
Structure of equine infectious anemia virus proteinase complexed with an inhibitor., Gustchina A, Kervinen J, Powell DJ, Zdanov A, Kay J, Wlodawer A, Protein Sci. 1996 Aug;5(8):1453-65. PMID:8844837
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