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1m8j

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(New page: 200px<br /><applet load="1m8j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m8j, resolution 2.40&Aring;" /> '''Crystal Structure Of...)
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[[Image:1m8j.gif|left|200px]]<br /><applet load="1m8j" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m8j, resolution 2.40&Aring;" />
 
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'''Crystal Structure Of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase Mutant R136A complexed with NAD'''<br />
 
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==Overview==
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==Crystal Structure Of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase Mutant R136A complexed with NAD==
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Several residues lining the ATP-binding site of Methanobacterium, thermoautotrophicum nicotinamide mononucleotide adenylyltransferase, (NMNATase) were mutated in an effort to better characterize their roles in, substrate binding and catalysis. Residues selected were Arg-11 and, Arg-136, both of which had previously been implicated as substrate binding, residues, as well as His-16 and His-19, part of the HXGH active site motif, and postulated to be of importance in catalysis. Kinetic studies revealed, that both Arg-11 and Arg-136 contributed to the binding of the substrate, ATP. When these amino acids were replaced by lysines, the apparent Km, values of the respective mutants for ATP decreased by factors of 1.3 and, 2.9 and by factors of 1.9 and 8.8 when the same residues were changed to, alanines. All four Arg mutants displayed unaltered Km values for NMN. The, apparent kcat values of the R11K and R136K mutants were the same as those, of WT NMNATase but the apparent kcat values of the alanine mutants had, decreased. Crystal structures of the Arg mutants revealed NAD+ and SO42-, molecules trapped at their active sites. The binding interactions of NAD+, were unchanged but the binding of SO42- was altered in these mutants, compared with wild type. The alanine mutants at positions His-16 and, His-19 retained approximately 6 and 1.3%, respectively, of WT NMNATase, activity indicating that His-19 is a key catalytic group. Surprisingly, this H19A mutant displayed a novel and distinct mode of NAD+ binding when, co-crystallized in the presence of NAD+ and SO42-.
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<StructureSection load='1m8j' size='340' side='right'caption='[[1m8j]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1m8j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M8J FirstGlance]. <br>
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1M8J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with SO4 and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M8J OCA].
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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]] 2.4&#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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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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=1m8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m8j OCA], [https://pdbe.org/1m8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m8j RCSB], [https://www.ebi.ac.uk/pdbsum/1m8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m8j ProSAT]</span></td></tr>
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Mutational, structural, and kinetic studies of the ATP-binding site of Methanobacterium thermoautotrophicum nicotinamide mononucleotide adenylyltransferase., Saridakis V, Pai EF, J Biol Chem. 2003 Sep 5;278(36):34356-63. Epub 2003 Jun 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12810729 12810729]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NADM_METTH NADM_METTH]
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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/m8/1m8j_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=1m8j ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Methanothermobacter thermautotrophicus]]
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[[Category: Nicotinamide-nucleotide adenylyltransferase]]
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[[Category: Pai EF]]
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[[Category: Single protein]]
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[[Category: Saridakis V]]
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[[Category: Pai, E.F.]]
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[[Category: Saridakis, V.]]
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[[Category: NAD]]
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[[Category: SO4]]
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[[Category: nucleotidyltransferase hxgh active site motif]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:13:51 2007''
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Current revision

Crystal Structure Of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase Mutant R136A complexed with NAD

PDB ID 1m8j

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