4a0h

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[[Image:4a0h.jpg|left|200px]]
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==Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana bound to 7-keto 8-amino pelargonic acid (KAPA)==
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<StructureSection load='4a0h' size='340' side='right' caption='[[4a0h]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4a0h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A0H FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KAP:7-KETO-8-AMINOPELARGONIC+ACID'>KAP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a0f|4a0f]], [[4a0g|4a0g]], [[4a0r|4a0r]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a0h RCSB], [http://www.ebi.ac.uk/pdbsum/4a0h PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/B0F481_ARATH B0F481_ARATH]] Bifunctional enzyme that catalyzes two different reactions involved in the biotin biosynthesis.<ref>PMID:17993549</ref> <ref>PMID:2909401</ref> <ref>PMID:16667573</ref> <ref>PMID:8676868</ref> Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring (By similarity).<ref>PMID:17993549</ref> <ref>PMID:2909401</ref> <ref>PMID:16667573</ref> <ref>PMID:8676868</ref> Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor.<ref>PMID:17993549</ref> <ref>PMID:2909401</ref> <ref>PMID:16667573</ref> <ref>PMID:8676868</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Diaminopelargonic acid aminotransferase (DAPA-AT) and dethiobiotin synthetase (DTBS) catalyze the antepenultimate and the penultimate steps, respectively, of biotin synthesis. Whereas DAPA-AT and DTBS are encoded by distinct genes in bacteria, in biotin-synthesizing eukaryotes (plants and most fungi), both activities are carried out by a single enzyme encoded by a bifunctional gene originating from the fusion of prokaryotic monofunctional ancestor genes. In few angiosperms, including Arabidopsis thaliana, this chimeric gene (named BIO3-BIO1) also produces a bicistronic transcript potentially encoding separate monofunctional proteins that can be produced following an alternative splicing mechanism. The functional significance of the occurrence of a bifunctional enzyme in biotin synthesis pathway in eukaryotes and the relative implication of each of the potential enzyme forms (bifunctional versus monofunctional) in the plant biotin pathway are unknown. In this study, we demonstrate that the BIO3-BIO1 fusion protein is the sole protein form produced by the BIO3-BIO1 locus in Arabidopsis. The enzyme catalyzes both DAPA-AT and DTBS reactions in vitro and is targeted to mitochondria in vivo. Our biochemical and kinetic characterizations of the pure recombinant enzyme show that in the course of the reaction, the DAPA intermediate is directly transferred from the DAPA-AT active site to the DTBS active site. Analysis of several structures of the enzyme crystallized in complex with and without its ligands reveals key structural elements involved for acquisition of bifunctionality and brings, together with mutagenesis experiments, additional evidences for substrate channeling.
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Biochemical and structural characterization of the Arabidopsis bifunctional enzyme dethiobiotin synthetase-diaminopelargonic Acid aminotransferase: evidence for substrate channeling in biotin synthesis.,Cobessi D, Dumas R, Pautre V, Meinguet C, Ferrer JL, Alban C Plant Cell. 2012 Apr;24(4):1608-25. Epub 2012 Apr 30. PMID:22547782<ref>PMID:22547782</ref>
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{{STRUCTURE_4a0h| PDB=4a0h | SCENE= }}
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===Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana bound to 7-keto 8-amino pelargonic acid (KAPA)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
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<!--
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*[[7%2C8-diaminopelargonic acid synthetase|7%2C8-diaminopelargonic acid synthetase]]
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The line below this paragraph, {{ABSTRACT_PUBMED_22547782}}, adds the Publication Abstract to the page
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== References ==
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(as it appears on PubMed at http://www.pubmed.gov), where 22547782 is the PubMed ID number.
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<references/>
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__TOC__
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{{ABSTRACT_PUBMED_22547782}}
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</StructureSection>
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==About this Structure==
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[[4a0h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A0H OCA].
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==Reference==
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<ref group="xtra">PMID:022547782</ref><references group="xtra"/>
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Alban, C.]]
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[[Category: Alban, C]]
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[[Category: Cobessi, D.]]
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[[Category: Cobessi, D]]
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[[Category: Dumas, R.]]
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[[Category: Dumas, R]]
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[[Category: Ferrer, J L.]]
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[[Category: Ferrer, J L]]
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[[Category: Meinguet, C.]]
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[[Category: Meinguet, C]]
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[[Category: Pautre, V.]]
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[[Category: Pautre, V]]
[[Category: Bio3-bio1]]
[[Category: Bio3-bio1]]
[[Category: Biotin synthesis]]
[[Category: Biotin synthesis]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 10:41, 4 January 2015

Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana bound to 7-keto 8-amino pelargonic acid (KAPA)

4a0h, resolution 2.81Å

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