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1dae

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DETHIOBIOTIN SYNTHETASE COMPLEXED WITH 3-(1-AMINOETHYL) NONANEDIOIC ACID

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dae"

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-[[Image:1dae.jpg|left|200px]]
- {{Structure
+==DETHIOBIOTIN SYNTHETASE COMPLEXED WITH 3-(1-AMINOETHYL) NONANEDIOIC ACID==
-|PDB= 1dae |SIZE=350|CAPTION= <scene name='initialview01'>1dae</scene>, resolution 1.70&Aring;
+<StructureSection load='1dae' size='340' side='right'caption='[[1dae]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=IKT:3-(1-AMINOETHYL)NONANEDIOIC+ACID'>IKT</scene>
+<table><tr><td colspan='2'>[[1dae]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DAE FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Dethiobiotin_synthase Dethiobiotin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.3.3 6.3.3.3] </span>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IKT:3-(1-AMINOETHYL)NONANEDIOIC+ACID'>IKT</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dae OCA], [https://pdbe.org/1dae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dae RCSB], [https://www.ebi.ac.uk/pdbsum/1dae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dae ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dae OCA], [http://www.ebi.ac.uk/pdbsum/1dae PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dae RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/BIOD1_ECOLI BIOD1_ECOLI] 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. Only CTP can partially replace ATP while diaminobiotin is only 37% as effective as 7,8-diaminopelargonic acid.<ref>PMID:4892372</ref> <ref>PMID:4921568</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/da/1dae_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </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/main_output.php?pdb_ID=1dae ConSurf].
+<div style="clear:both"></div>
-'''DETHIOBIOTIN SYNTHETASE COMPLEXED WITH 3-(1-AMINOETHYL) NONANEDIOIC ACID'''
+==See Also==
+*[[Dethiobiotin synthetase 3D structures|Dethiobiotin synthetase 3D structures]]
+== References ==
-==Overview==
+<references/>
-The crystal structures of six complexes of homodimeric Escherichia coli dethiobiotin synthetase with a variety of substrates, substrate analogs, and products have been determined to high resolution. These include (1) the binary complex of dethiobiotin synthetase and the N7-carbamate of 7,8-diaminononanoic acid, (2) the binary complex of enzyme and the alternate substrate, 3-(1-aminoethyl)-nonanedioic acid, (3) the binary complex of enzyme with the product ADP, (4) the quaternary complex of enzyme, ADP, the N7-carbamate of 7,8-diaminononanoic acid, and Ca2+, (5) the ternary complex of enzyme, the ATP analog adenylyl (beta, gamma-methylene)diphosphonate, and the N7-carbamate of 7,8-diaminononanoic acid, and (6) the quaternary complex of enzyme, the ATP analog adenylyl (beta, gamma-methylene)diphosphonate, 7,8-diaminononanoic acid, and Mn2+. One molecule of each substrate binds to one monomer of the enzyme. ADP and the ATP analogue bind to the classical mononucleotide binding fold with the phosphate groups close to the phosphate binding loop Gly8--Thr16 between beta-strand beta 1 and the N-terminus of alpha-helix alpha 1. The adenine ring is bound in a pocket between beta-strands beta 6 and beta 7. In the quaternary complex with Mn2+, the metal binding site is found in the vicinity of the beta- and gamma-phosphate groups. Two oxygen atoms from the phosphates and oxygen atoms from the side chains of Asp54, Thr16, and Glu115 are ligands to the Mn2+ ion in the quaternary complex. In the complex with ADP and the N7-carbamate of 7,8-diaminononanoic acid prepared in the presence of Ca2+ ions, a different metal binding site is found. The Ca2+ ion is coordinated to an oxygen atom of the alpha-phosphate group of the nucleotide, the side chain of Asp54, and solvent molecules. The 7,8-diaminononanoic acid substrate molecule interacts with residues from both subunits, making the dimer the minimal functional unit. The diamino group binds between the loops after beta 2 and beta 4, and the terminal carboxyl group at the hydrophobic tail of the substrate interacts with the amino terminus of helix alpha 5 and with the side chain of Tyr187 in helix alpha 6 of the second subunit at the monomer-monomer interface. Strong additional electron density close to the N7 nitrogen atom of the 7,8-diaminononanoic acid substrate in some complexes indicates that, even in the absence of added bicarbonate in the crystallization mixture, the carbamylated intermediate is formed in the crystal.(ABSTRACT TRUNCATED AT 400 WORDS)
+__TOC__
+</StructureSection>
-==About this Structure==
-DAE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DAE OCA].
-==Reference==
-Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate., Huang W, Jia J, Gibson KJ, Taylor WS, Rendina AR, Schneider G, Lindqvist Y, Biochemistry. 1995 Sep 5;34(35):10985-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7669756 7669756]
-[[Category: Dethiobiotin synthase]]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Huang, W.]]
+[[Category: Huang W]]
-[[Category: Jia, J.]]
+[[Category: Jia J]]
-[[Category: Lindqvist, Y.]]
+[[Category: Lindqvist Y]]
-[[Category: Schneider, G.]]
+[[Category: Schneider G]]
-[[Category: atp-binding]]
-[[Category: biotin biosynthesis]]
-[[Category: ligase]]
-[[Category: magnesium]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:37:44 2008''

1dae

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DETHIOBIOTIN SYNTHETASE COMPLEXED WITH 3-(1-AMINOETHYL) NONANEDIOIC ACID

Structural highlights

Function

Evolutionary Conservation

See Also

References

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