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| | <StructureSection load='1t2b' size='340' side='right'caption='[[1t2b]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='1t2b' size='340' side='right'caption='[[1t2b]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1t2b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51113 Atcc 51113]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1T2B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1t2b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_braakii Citrobacter braakii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T2B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CNL:1,3,3-TRIMETHYL-2-OXABICYCLO[2.2.2]OCTANE'>CNL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cinA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=57706 ATCC 51113])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CNL:1,3,3-TRIMETHYL-2-OXABICYCLO[2.2.2]OCTANE'>CNL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1t2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2b OCA], [http://pdbe.org/1t2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t2b RCSB], [http://www.ebi.ac.uk/pdbsum/1t2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t2b ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2b OCA], [https://pdbe.org/1t2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t2b RCSB], [https://www.ebi.ac.uk/pdbsum/1t2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t2b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CINA_CITBR CINA_CITBR]] Involved in the degradation of cineol (eucalyptol). Catalyzes the initial hydroxylation of cineole exclusively at the pro-R carbon to give the (S)-6beta-hydroxycineole. Cineole is the natural substrate of CinA. | + | [https://www.uniprot.org/uniprot/CINA_CITBR CINA_CITBR] Involved in the degradation of cineol (eucalyptol). Catalyzes the initial hydroxylation of cineole exclusively at the pro-R carbon to give the (S)-6beta-hydroxycineole. Cineole is the natural substrate of CinA. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 51113]] | + | [[Category: Citrobacter braakii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hawkes, D B]] | + | [[Category: De Voss J]] |
| - | [[Category: Li, H]] | + | [[Category: Hawkes DB]] |
| - | [[Category: Meharenna, Y T]] | + | [[Category: Li H]] |
| - | [[Category: Pearson, A G]] | + | [[Category: Meharenna YT]] |
| - | [[Category: Poulos, T L]] | + | [[Category: Pearson AG]] |
| - | [[Category: Voss, J De]] | + | [[Category: Poulos TL]] |
| - | [[Category: B'-helix]]
| + | |
| - | [[Category: Loop]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
CINA_CITBR Involved in the degradation of cineol (eucalyptol). Catalyzes the initial hydroxylation of cineole exclusively at the pro-R carbon to give the (S)-6beta-hydroxycineole. Cineole is the natural substrate of CinA.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cytochrome P450cin catalyzes the monooxygenation of 1,8-cineole, which is structurally very similar to d-camphor, the substrate for the most thoroughly investigated cytochrome P450, cytochrome P450cam. Both 1,8-cineole and d-camphor are C(10) monoterpenes containing a single oxygen atom with very similar molecular volumes. The cytochrome P450cin-substrate complex crystal structure has been solved to 1.7 A resolution and compared with that of cytochrome P450cam. Despite the similarity in substrates, the active site of cytochrome P450cin is substantially different from that of cytochrome P450cam in that the B' helix, essential for substrate binding in many cytochrome P450s including cytochrome P450cam, is replaced by an ordered loop that results in substantial changes in active site topography. In addition, cytochrome P450cin does not have the conserved threonine, Thr252 in cytochrome P450cam, which is generally considered as an integral part of the proton shuttle machinery required for oxygen activation. Instead, the analogous residue in cytochrome P450cin is Asn242, which provides the only direct protein H-bonding interaction with the substrate. Cytochrome P450cin uses a flavodoxin-like redox partner to reduce the heme iron rather than the more traditional ferredoxin-like Fe(2)S(2) redox partner used by cytochrome P450cam and many other bacterial P450s. It thus might be expected that the redox partner docking site of cytochrome P450cin would resemble that of cytochrome P450BM3, which also uses a flavodoxin-like redox partner. Nevertheless, the putative docking site topography more closely resembles cytochrome P450cam than cytochrome P450BM3.
Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450cam.,Meharenna YT, Li H, Hawkes DB, Pearson AG, De Voss J, Poulos TL Biochemistry. 2004 Jul 27;43(29):9487-94. PMID:15260491[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Meharenna YT, Li H, Hawkes DB, Pearson AG, De Voss J, Poulos TL. Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450cam. Biochemistry. 2004 Jul 27;43(29):9487-94. PMID:15260491 doi:10.1021/bi049293p
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