1n5t

<StructureSection load='1n5t' size='340' side='right' caption='[[1n5t]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[1n5t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N5T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N5T FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OAL:(1,8-DIHYDROXY-9,10-DIOXO-9,10-DIHYDRO-ANTHRACEN-2-YL)-ACETIC+ACID'>OAL</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lq9|1lq9]], [[1n5q|1n5q]], [[1n5s|1n5s]], [[1n5v|1n5v]]</td></tr>

<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ActVA-Orf6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 Streptomyces coelicolor])</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n5t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n5t RCSB], [http://www.ebi.ac.uk/pdbsum/1n5t PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/1n5t_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

ActVA-Orf6 monooxygenase from Streptomyces coelicolor that catalyses the oxidation of an aromatic intermediate of the actinorhodin biosynthetic pathway is a member of a class of small monooxygenases that carry out oxygenation without the assistance of any of the prosthetic groups, metal ions or cofactors normally associated with activation of molecular oxygen. The overall structure is a ferredoxin-like fold with a novel dimeric assembly, indicating that the widely represented ferredoxin fold may sustain yet another functionality. The resolution (1.3 A) of the enzyme structure and its complex with substrate and product analogues allows us to visualize the mechanism of binding and activation of the substrate for attack by molecular oxygen, and utilization of two gates for the reaction components including a proton gate and an O(2)/H(2)O gate with a putative protein channel. This is the first crystal structure of an enzyme involved in the tailoring of a type II aromatic polyketide and illustrates some of the enzyme-substrate recognition features that may apply to a range of other enzymes involved in modifying a polyketide core structure.

The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.,Sciara G, Kendrew SG, Miele AE, Marsh NG, Federici L, Malatesta F, Schimperna G, Savino C, Vallone B EMBO J. 2003 Jan 15;22(2):205-15. PMID:12514126<ref>PMID:12514126</ref>

== References ==

[[Category: Streptomyces coelicolor]]

[[Category: Federici, L.]]

[[Category: Kendrew, S G.]]

[[Category: Malatesta, F.]]

[[Category: Marsh, N G.]]

[[Category: Miele, A E.]]

[[Category: Savino, C.]]

[[Category: Schimperna, G.]]

[[Category: Sciara, G.]]

[[Category: Vallone, B.]]

[[Category: Streptomyces coelicolor]]