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New page: left|200px<br /><applet load="1mlz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mlz, resolution 2.15Å" /> '''Crystal Structure of...
 
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[[Image:1mlz.gif|left|200px]]<br /><applet load="1mlz" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mlz, resolution 2.15&Aring;" />
'''Crystal Structure of 7,8-Diaminopelargonic Acid Synthase in complex with the trans-isomer of amiclenomycin.'''<br />


==Overview==
==Crystal Structure of 7,8-Diaminopelargonic Acid Synthase in complex with the trans-isomer of amiclenomycin.==
The antibiotic amiclenomycin blocks the biosynthesis of biotin by, inhibiting the pyridoxal-phosphate-dependent enzyme diaminopelargonic acid, synthase. Inactivation of the enzyme is stereoselective, i.e. the cis, isomer of amiclenomycin is a potent inhibitor, whereas the trans isomer is, much less reactive. The crystal structure of the complex of the holoenzyme, and amiclenomycin at 1.8 A resolution reveals that the internal aldimine, linkage between the cofactor and the side chain of the catalytic residue, Lys-274 is broken. Instead, a covalent bond is formed between the 4-amino, nitrogen of amiclenomycin and the C4' carbon atom of pyridoxal-phosphate., The electron density for the bound inhibitor suggests that aromatization, of the cyclohexadiene ring has occurred upon formation of the covalent, adduct. This process could be initiated by proton abstraction at the C4, carbon atom of the cyclohexadiene ring, possibly by the proximal side, chain of Lys-274, leading to the tautomer Schiff base followed by the, removal of the second allylic hydrogen. The carboxyl tail of the, amiclenomycin moiety forms a salt link to the conserved residue Arg-391 in, the substrate-binding site. Modeling suggests steric hindrance at the, active site as the determinant of the weak inhibiting potency of the trans, isomer.
<StructureSection load='1mlz' size='340' side='right'caption='[[1mlz]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mlz]] is a 2 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=1MLZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MLZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=TZA:TRANS-AMICLENOMYCIN'>TZA</scene></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=1mlz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mlz OCA], [https://pdbe.org/1mlz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mlz RCSB], [https://www.ebi.ac.uk/pdbsum/1mlz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mlz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BIOA_ECOLI BIOA_ECOLI] 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:1092681</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/ml/1mlz_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=1mlz ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1MLZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with TZA, NA and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosylmethionine--8-amino-7-oxononanoate_transaminase Adenosylmethionine--8-amino-7-oxononanoate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.62 2.6.1.62] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MLZ OCA].
*[[7%2C8-diaminopelargonic acid synthase 3D structures|7%2C8-diaminopelargonic acid synthase 3D structures]]
 
== References ==
==Reference==
<references/>
Structural basis for the inhibition of the biosynthesis of biotin by the antibiotic amiclenomycin., Sandmark J, Mann S, Marquet A, Schneider G, J Biol Chem. 2002 Nov 8;277(45):43352-8. Epub 2002 Sep 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12218056 12218056]
__TOC__
[[Category: Adenosylmethionine--8-amino-7-oxononanoate transaminase]]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Mann, S.]]
[[Category: Mann S]]
[[Category: Marquet, A.]]
[[Category: Marquet A]]
[[Category: Sandmark, J.]]
[[Category: Sandmark J]]
[[Category: Schneider, G.]]
[[Category: Schneider G]]
[[Category: NA]]
[[Category: PLP]]
[[Category: TZA]]
[[Category: amiclenomycin]]
[[Category: aminotransferase]]
[[Category: fold type i]]
[[Category: subclass ii]]
 
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Retrieved from "https://proteopedia.org/1mlz"