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1rqn

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[[Image:1rqn.gif|left|200px]]
 
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{{Structure
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==Phosphonoacetaldehyde hydrolase complexed with magnesium==
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|PDB= 1rqn |SIZE=350|CAPTION= <scene name='initialview01'>1rqn</scene>, resolution 2.80&Aring;
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<StructureSection load='1rqn' size='340' side='right'caption='[[1rqn]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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<table><tr><td colspan='2'>[[1rqn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RQN FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.8&#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=MG:MAGNESIUM+ION'>MG</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=1rqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rqn OCA], [https://pdbe.org/1rqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rqn RCSB], [https://www.ebi.ac.uk/pdbsum/1rqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rqn ProSAT]</span></td></tr>
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</table>
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'''Phosphonoacetaldehyde hydrolase complexed with magnesium'''
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== Function ==
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[https://www.uniprot.org/uniprot/PHNX_BACCE PHNX_BACCE] Involved in phosphonate degradation.
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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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Phosphonoacetaldehyde hydrolase (phosphonatase) catalyzes the hydrolytic P-C bond cleavage of phosphonoacetaldehyde (Pald) to form orthophosphate and acetaldehyde. The reaction proceeds via a Schiff-base intermediate formed between Lys-53 and the Pald carbonyl. The x-ray crystal structures of the wild-type phosphonatase complexed with Mg(II) alone or with Mg(II) plus vinylsulfonate (a phosphonoethylenamine analog) were determined to 2.8 and 2.4 A, respectively. These structures were used to determine the identity and positions of active site residues surrounding the Lys-53 ammonium group and the Pald carbonyl. These include Cys-22, His-56, Tyr-128, and Met-49. Site-directed mutagenesis was then employed to determine whether or not these groups participate in catalysis. Based on rate contributions, Tyr-128 and Cys-22 were eliminated as potential catalytic groups. The Lys-53 epsilon-amino group, positioned for reaction with the Pald carbonyl, forms a hydrogen bond with water 120. Water 120 is also within hydrogen bond distance of an imidazole nitrogen of His-56 and the sulfur atom of Met-49. Kinetic constants for mutants indicated that His-56 (1000-fold reduction in k(cat)/K(m) upon Ala substitution) and Met-49 (17,000-fold reduction in k(cat)/K(m) upon Leu substitution) function in catalysis of Schiff-base formation. Based on these results, it is proposed that a network of hydrogen bonds among Lys-53, water 120, His-56, and Met-49 facilitate proton transfer from Lys-53 to the carbinolamine intermediate. Comparison of the vinylsulfonate complex versus unliganded structures indicated that association of the cap and core domains is essential for the positioning of the Lys-53 for attack at the Pald carbonyl and that substrate binding at the core domain stabilizes cap domain binding.
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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/rq/1rqn_consurf.spt"</scriptWhenChecked>
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1RQN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQN 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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X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis., Morais MC, Zhang G, Zhang W, Olsen DB, Dunaway-Mariano D, Allen KN, J Biol Chem. 2004 Mar 5;279(10):9353-61. Epub 2003 Dec 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14670958 14670958]
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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=1rqn ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Allen, K N.]]
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[[Category: Allen KN]]
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[[Category: Dunaway-Mariano, D.]]
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[[Category: Dunaway-Mariano D]]
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[[Category: Morais, M C.]]
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[[Category: Morais MC]]
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[[Category: Olsen, D B.]]
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[[Category: Olsen DB]]
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[[Category: Zhang, G.]]
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[[Category: Zhang G]]
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[[Category: Zhang, W.]]
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[[Category: Zhang W]]
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[[Category: MG]]
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[[Category: schiff-base formation; acid/base catalysis; structural enzymology; had superfamily]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:55:02 2008''
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Current revision

Phosphonoacetaldehyde hydrolase complexed with magnesium

PDB ID 1rqn

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