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1m9d

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[[Image:1m9d.gif|left|200px]]<br />
 
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<applet load="1m9d" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m9d, resolution 1.900&Aring;" />
 
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'''X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) O-type chimera Complex.'''<br />
 
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==Overview==
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==X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) O-type chimera Complex.==
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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.
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<StructureSection load='1m9d' size='340' side='right'caption='[[1m9d]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1m9d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M9D FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9d OCA], [https://pdbe.org/1m9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m9d RCSB], [https://www.ebi.ac.uk/pdbsum/1m9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m9d ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m9/1m9d_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m9d ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1M9D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M9D OCA].
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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==Reference==
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__TOC__
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12730686 12730686]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Hill CP]]
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[[Category: Hill, C.P.]]
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[[Category: Howard BR]]
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[[Category: Howard, B.R.]]
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[[Category: Li S]]
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[[Category: Li, S.]]
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[[Category: Sundquist WI]]
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[[Category: Sundquist, W.I.]]
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[[Category: Vajdos FF]]
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[[Category: Vajdos, F.F.]]
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[[Category: capsid]]
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[[Category: cyclophilin a]]
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[[Category: hiv-1]]
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[[Category: isomerase]]
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[[Category: rotamase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:09:02 2007''
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Current revision

X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) O-type chimera Complex.

PDB ID 1m9d

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