1m9e: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span> | ||
|GENE= CA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1]) | |GENE= CA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1ak4|1AK4]], [[1m96|1M96]], [[1m9c|1M9C]], [[1m9d|1M9D]], [[1m9f|1M9F]], [[1m9x|1M9X]], [[1m9y|1M9Y]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9e OCA], [http://www.ebi.ac.uk/pdbsum/1m9e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m9e RCSB]</span> | |||
}} | }} | ||
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[[Category: rotamase]] | [[Category: rotamase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:13:03 2008'' | ||
Revision as of 19:13, 30 March 2008
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| 1m9e, resolution 1.72Å | |||||||||||||
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| Gene: | CA (Human immunodeficiency virus 1) | ||||||||||||
| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||||||||
| Related: | 1AK4, 1M96, 1M9C, 1M9D, 1M9F, 1M9X, 1M9Y
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A Complex.
Overview
Cyclophilins constitute a ubiquitous protein family whose functions include protein folding, transport and signaling. They possess both sequence-specific binding and proline cis-trans isomerase activities, as exemplified by the interaction between cyclophilin A (CypA) and the HIV-1 CA protein. Here, we report crystal structures of CypA in complex with HIV-1 CA protein variants that bind preferentially with the substrate proline residue in either the cis or the trans conformation. Cis- and trans-Pro substrates are accommodated within the enzyme active site by rearrangement of their N-terminal residues and with minimal distortions in the path of the main chain. CypA Arg55 guanidinium group probably facilitates catalysis by anchoring the substrate proline oxygen and stabilizing sp3 hybridization of the proline nitrogen in the transition state.
About this Structure
1M9E is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Structural insights into the catalytic mechanism of cyclophilin A., Howard BR, Vajdos FF, Li S, Sundquist WI, Hill CP, Nat Struct Biol. 2003 Jun;10(6):475-81. PMID:12730686
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