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1ct9

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[[Image:1ct9.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLI==
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|PDB= 1ct9 |SIZE=350|CAPTION= <scene name='initialview01'>1ct9</scene>, resolution 2.00&Aring;
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<StructureSection load='1ct9' size='340' side='right'caption='[[1ct9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>
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<table><tr><td colspan='2'>[[1ct9]] is a 4 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=1CT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CT9 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Asparagine_synthase_(glutamine-hydrolyzing) Asparagine synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.4 6.3.5.4]
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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&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=IUM:URANYL+(VI)+ION'>IUM</scene></td></tr>
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}}
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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=1ct9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ct9 OCA], [https://pdbe.org/1ct9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ct9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ct9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ct9 ProSAT]</span></td></tr>
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</table>
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'''CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLI'''
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== Function ==
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[https://www.uniprot.org/uniprot/ASNB_ECOLI ASNB_ECOLI] Catalyzes the ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen. Can also use ammonia as the nitrogen source in vitro, albeit with lower efficiency. As nucleotide substrates, ATP and dATP are utilized at a similar rate in both the glutamine- and ammonia-dependent reactions, whereas GTP utilization is only 15% that of ATP, and CTP, UTP, ITP and XTP are very poor or not substrates. Also exhibits glutaminase activity.<ref>PMID:7907328</ref> <ref>PMID:6102982</ref> <ref>PMID:20853825</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Asparagine synthetase B catalyzes the assembly of asparagine from aspartate, Mg(2+)ATP, and glutamine. Here, we describe the three-dimensional structure of the enzyme from Escherichia colidetermined and refined to 2.0 A resolution. Protein employed for this study was that of a site-directed mutant protein, Cys1Ala. Large crystals were grown in the presence of both glutamine and AMP. Each subunit of the dimeric protein folds into two distinct domains. The N-terminal region contains two layers of antiparallel beta-sheet with each layer containing six strands. Wedged between these layers of sheet is the active site responsible for the hydrolysis of glutamine. Key side chains employed for positioning the glutamine substrate within the binding pocket include Arg 49, Asn 74, Glu 76, and Asp 98. The C-terminal domain, responsible for the binding of both Mg(2+)ATP and aspartate, is dominated by a five-stranded parallel beta-sheet flanked on either side by alpha-helices. The AMP moiety is anchored to the protein via hydrogen bonds with O(gamma) of Ser 346 and the backbone carbonyl and amide groups of Val 272, Leu 232, and Gly 347. As observed for other amidotransferases, the two active sites are connected by a tunnel lined primarily with backbone atoms and hydrophobic and nonpolar amino acid residues. Strikingly, the three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ct/1ct9_consurf.spt"</scriptWhenChecked>
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1CT9 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=1CT9 OCA].
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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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==Reference==
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</jmolCheckbox>
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Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product., Larsen TM, Boehlein SK, Schuster SM, Richards NG, Thoden JB, Holden HM, Rayment I, Biochemistry. 1999 Dec 7;38(49):16146-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10587437 10587437]
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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=1ct9 ConSurf].
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[[Category: Asparagine synthase (glutamine-hydrolyzing)]]
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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: Boehlein, S K.]]
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[[Category: Boehlein SK]]
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[[Category: Holden, H M.]]
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[[Category: Holden HM]]
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[[Category: Larsen, T M.]]
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[[Category: Larsen TM]]
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[[Category: Rayment, I.]]
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[[Category: Rayment I]]
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[[Category: Richards, N G.J.]]
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[[Category: Richards NGJ]]
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[[Category: Schuster, S M.]]
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[[Category: Schuster SM]]
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[[Category: Thoden, J B.]]
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[[Category: Thoden JB]]
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[[Category: AMP]]
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[[Category: CL]]
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[[Category: GLN]]
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[[Category: IUM]]
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[[Category: amidotransferase]]
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[[Category: asparagine biosynthesis]]
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[[Category: substrate channeling]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:28:37 2008''
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Current revision

CRYSTAL STRUCTURE OF ASPARAGINE SYNTHETASE B FROM ESCHERICHIA COLI

PDB ID 1ct9

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