1mgv

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[[Image:1mgv.gif|left|200px]]
 
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==Crystal Structure of the R391A Mutant of 7,8-Diaminopelargonic Acid Synthase==
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The line below this paragraph, containing "STRUCTURE_1mgv", creates the "Structure Box" on the page.
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<StructureSection load='1mgv' size='340' side='right'caption='[[1mgv]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1mgv]] 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=1MGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MGV FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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{{STRUCTURE_1mgv| PDB=1mgv | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgv OCA], [https://pdbe.org/1mgv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mgv RCSB], [https://www.ebi.ac.uk/pdbsum/1mgv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mgv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mg/1mgv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1mgv ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of the R391A Mutant of 7,8-Diaminopelargonic Acid Synthase'''
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==See Also==
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*[[7%2C8-diaminopelargonic acid synthase 3D structures|7%2C8-diaminopelargonic acid synthase 3D structures]]
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== References ==
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==Overview==
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<references/>
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7,8-diaminopelargonic acid (DAPA) synthase (EC 2.6.1.62) is a pyridoxal phosphate (PLP)-dependent transaminase that catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form DAPA in the antepenultimate step in the biosynthesis of biotin. The wild-type enzyme has a steady-state kcat value of 0.013 s(-1), and the K(m) values for SAM and KAPA are 150 and &lt;2 microM, respectively. The k(max) and apparent K(m) values for the half-reaction of the PLP form of the enzyme with SAM are 0.016 s(-1) and 300 microM, respectively, while those for the reaction with DAPA are 0.79 s(-1) and 1 microM. The R391A mutant enzyme exhibits near wild-type kinetic parameters in the reaction with SAM, while the apparent K(m) for DAPA is increased 180-fold. The 2.1 A crystal structure of the R391A mutant enzyme shows that the mutation does not significantly alter the structure. These results indicate that the conserved arginine residue is not required for binding the alpha-amino acid SAM, but it is important for recognition of DAPA.
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__TOC__
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</StructureSection>
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==About this Structure==
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1MGV 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=1MGV OCA].
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==Reference==
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The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation., Eliot AC, Sandmark J, Schneider G, Kirsch JF, Biochemistry. 2002 Oct 22;41(42):12582-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12379100 12379100]
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[[Category: Adenosylmethionine--8-amino-7-oxononanoate transaminase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Eliot, A C.]]
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[[Category: Eliot AC]]
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[[Category: Kirsch, J F.]]
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[[Category: Kirsch JF]]
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[[Category: Sandmark, J.]]
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[[Category: Sandmark J]]
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[[Category: Schneider, G.]]
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[[Category: Schneider G]]
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[[Category: Aminotransferase]]
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[[Category: Fold type i]]
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[[Category: Homodimer]]
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[[Category: Subclass ii]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:00:16 2008''
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Current revision

Crystal Structure of the R391A Mutant of 7,8-Diaminopelargonic Acid Synthase

PDB ID 1mgv

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