This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2ipi
From Proteopedia
(Difference between revisions)
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==Crystal Structure of Aclacinomycin Oxidoreductase== | ==Crystal Structure of Aclacinomycin Oxidoreductase== | ||
| - | <StructureSection load='2ipi' size='340' side='right' caption='[[2ipi]], [[Resolution|resolution]] 1.65Å' scene=''> | + | <StructureSection load='2ipi' size='340' side='right'caption='[[2ipi]], [[Resolution|resolution]] 1.65Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2ipi]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2ipi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/As_4.1320 As 4.1320]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IPI FirstGlance]. <br> |
| - | <b>[[Ligand|Ligands:]]</b> <scene name='pdbligand=AKY:METHYL+(2S,4R)-2-ETHYL-2,5,7-TRIHYDROXY-6,11-DIOXO-4-{[2,3,6-TRIDEOXY-4-O-{2,6-DIDEOXY-4-O-[(2S,6S)-6-METHYL-5-OXOTETRAHYDRO-2H-PYRAN-2-YL]-ALPHA-D-LYXO-HEXOPYRANOSYL}-3-(DIMETHYLAMINO)-D-RIBO-HEXOPYRANOSYL]OXY}-1,2,3,4,6,11-HEXAHYDROTETRACENE-1-CARBOXYLATE'>AKY</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKY:METHYL+(2S,4R)-2-ETHYL-2,5,7-TRIHYDROXY-6,11-DIOXO-4-{[2,3,6-TRIDEOXY-4-O-{2,6-DIDEOXY-4-O-[(2S,6S)-6-METHYL-5-OXOTETRAHYDRO-2H-PYRAN-2-YL]-ALPHA-D-LYXO-HEXOPYRANOSYL}-3-(DIMETHYLAMINO)-D-RIBO-HEXOPYRANOSYL]OXY}-1,2,3,4,6,11-HEXAHYDROTETRACENE-1-CARBOXYLATE'>AKY</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <b> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AknOx ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33899 AS 4.1320])</td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ipi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ipi OCA], [https://pdbe.org/2ipi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ipi RCSB], [https://www.ebi.ac.uk/pdbsum/2ipi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ipi ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/AKNOX_STRGJ AKNOX_STRGJ]] Involved in the modification of the terminal sugar residues in the last two steps in the biosynthesis of polyketide antibiotics of the aclacinomycin group. In the first reaction, it catalyzes the oxidation of the hydroxyl group at carbon C4 of the L-rhodinose terminal sugar moiety of aclacinomycin N (AclN) to a keto group, modifying the sugar to cinerulose A and generating aclacinomycin A (AclA). In the second reaction, it catalyzes the elimination of two hydrogen atoms from cinerulose A, leading to a double bond between carbon atoms C2 and C3 and the generation of the L-aculose terminal sugar moiety of aclacinomycin Y (AclY). It can also use aclacinomycin analogs, epsilon-pyrromycinone glycosides, rhodirubins (A, B, C and E) and all triglycosides containing L-cinerulose, L-rhodinose or 2-deoxy-L-fucose as terminal sugar.<ref>PMID:12137949</ref> <ref>PMID:17395717</ref> <ref>PMID:528393</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| - | [[Image:Consurf_key_small.gif|right]] | + | [[Image:Consurf_key_small.gif|200px|right]] |
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ip/2ipi_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ip/2ipi_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=2ipi ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
The crystal structure of aclacinomycin oxidoreductase (AknOx), a tailoring enzyme involved in the biosynthesis of the polyketide antibiotic aclacinomycin, was determined to 1.65 A resolution by multiwavelength anomalous diffraction using data from selenomethionine-substituted crystals. The crystals belong to space group P2(1), with unit-cell parameters a = 68.2, b = 264.5, c = 68.2 A, beta = 119 degrees . Analysis of the intensity statistics clearly showed the presence of pseudomerohedral twinning. The data set could also be indexed and scaled with an R(sym) of 0.072 in the orthorhombic space group C222(1) (unit-cell parameters a = 69.7, b = 117.5, c = 264.4 A), indicating the possibility of pseudomerohedral twinning along the diagonal between the monoclinic a and c directions. Refinement using this twin operator resulted in an R(free) of 24.2%. A monoclinic lattice with a = c and beta close to 120 degrees can emulate a hexagonal metric, with the possibility of a threefold twin operator along the b axis and three twin domains. Refinement assuming three-domain twinning gave a final R(free) of 26.5%. The structure of AknOx can be thus refined with comparable R(free) values using either of the twin operators separately, suggesting the possibility that crystals of AknOx contain six twin domains generated by the twofold and threefold twin operators perpendicular to each other. Both twin operators coincide with noncrystallographic symmetry axes that may promote twinning. | The crystal structure of aclacinomycin oxidoreductase (AknOx), a tailoring enzyme involved in the biosynthesis of the polyketide antibiotic aclacinomycin, was determined to 1.65 A resolution by multiwavelength anomalous diffraction using data from selenomethionine-substituted crystals. The crystals belong to space group P2(1), with unit-cell parameters a = 68.2, b = 264.5, c = 68.2 A, beta = 119 degrees . Analysis of the intensity statistics clearly showed the presence of pseudomerohedral twinning. The data set could also be indexed and scaled with an R(sym) of 0.072 in the orthorhombic space group C222(1) (unit-cell parameters a = 69.7, b = 117.5, c = 264.4 A), indicating the possibility of pseudomerohedral twinning along the diagonal between the monoclinic a and c directions. Refinement using this twin operator resulted in an R(free) of 24.2%. A monoclinic lattice with a = c and beta close to 120 degrees can emulate a hexagonal metric, with the possibility of a threefold twin operator along the b axis and three twin domains. Refinement assuming three-domain twinning gave a final R(free) of 26.5%. The structure of AknOx can be thus refined with comparable R(free) values using either of the twin operators separately, suggesting the possibility that crystals of AknOx contain six twin domains generated by the twofold and threefold twin operators perpendicular to each other. Both twin operators coincide with noncrystallographic symmetry axes that may promote twinning. | ||
| Line 21: | Line 26: | ||
Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning.,Sultana A, Alexeev I, Kursula I, Mantsala P, Niemi J, Schneider G Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):149-59. Epub 2007, Jan 16. PMID:17242508<ref>PMID:17242508</ref> | Structure determination by multiwavelength anomalous diffraction of aclacinomycin oxidoreductase: indications of multidomain pseudomerohedral twinning.,Sultana A, Alexeev I, Kursula I, Mantsala P, Niemi J, Schneider G Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):149-59. Epub 2007, Jan 16. PMID:17242508<ref>PMID:17242508</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2ipi" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: As 4 1320]] |
| - | [[Category: Alexeev, I | + | [[Category: Large Structures]] |
| - | [[Category: Kursula, I | + | [[Category: Alexeev, I]] |
| - | [[Category: Mantsala, P | + | [[Category: Kursula, I]] |
| - | [[Category: Niemi, J | + | [[Category: Mantsala, P]] |
| - | [[Category: Schneider, G | + | [[Category: Niemi, J]] |
| - | [[Category: Sultana, A | + | [[Category: Schneider, G]] |
| + | [[Category: Sultana, A]] | ||
[[Category: Aclacinomycin]] | [[Category: Aclacinomycin]] | ||
[[Category: Anthracycline]] | [[Category: Anthracycline]] | ||
Current revision
Crystal Structure of Aclacinomycin Oxidoreductase
| |||||||||||
Categories: As 4 1320 | Large Structures | Alexeev, I | Kursula, I | Mantsala, P | Niemi, J | Schneider, G | Sultana, A | Aclacinomycin | Anthracycline | Flavoenzyme | Mad | Oxidoreductase | Twinning
