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2aaj

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(New page: 200px<br /><applet load="2aaj" size="350" color="white" frame="true" align="right" spinBox="true" caption="2aaj, resolution 2.74&Aring;" /> '''Crystal Structures o...)
Current revision (09:12, 14 February 2024) (edit) (undo)
 
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[[Image:2aaj.gif|left|200px]]<br /><applet load="2aaj" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2aaj, resolution 2.74&Aring;" />
 
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'''Crystal Structures of the Wild-type, Mutant-P1A and Inactivated Malonate Semialdehyde Decarboxylase: A Structural Basis for the Decarboxylase and Hydratase Activities'''<br />
 
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==Overview==
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==Crystal Structures of the Wild-type, Mutant-P1A and Inactivated Malonate Semialdehyde Decarboxylase: A Structural Basis for the Decarboxylase and Hydratase Activities==
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Malonate semialdehyde decarboxylase (MSAD) from Pseudomonas pavonaceae 170, is a tautomerase superfamily member that converts malonate semialdehyde to, acetaldehyde by a mechanism utilizing Pro-1 and Arg-75. Pro-1 and Arg-75, have also been implicated in the hydratase activity of MSAD in which, 2-oxo-3-pentynoate is processed to acetopyruvate. Crystal structures of, MSAD (1.8 A resolution), the P1A mutant of MSAD (2.7 A resolution), and, MSAD inactivated by 3-chloropropiolate (1.6 A resolution), a, mechanism-based inhibitor activated by the hydratase activity of MSAD, have been determined. A comparison of the P1A-MSAD and MSAD structures, reveals little geometric alteration, indicating that Pro-1 plays an, important catalytic role but not a critical structural role. The, structures of wild-type MSAD and MSAD covalently modified at Pro-1 by, 3-oxopropanoate, the adduct resulting from the incubation of MSAD and, 3-chloropropiolate, implicate Asp-37 as the residue that activates a water, molecule for attack at C-3 of 3-chloropropiolate to initiate a Michael, addition of water. The interactions of Arg-73 and Arg-75 with the C-1, carboxylate group of the adduct suggest these residues polarize the, alpha,beta-unsaturated acid and facilitate the addition of water. On the, basis of these structures, a mechanism for the inactivation of MSAD by, 3-chloropropiolate can be formulated along with mechanisms for the, decarboxylase and hydratase activities. The results also provide, additional evidence supporting the hypothesis that MSAD and, trans-3-chloroacrylic acid dehalogenase, a tautomerase superfamily member, preceding MSAD in the trans-1,3-dichloropropene degradation pathway, diverged from a common ancestor but retained the key elements for the, conjugate addition of water.
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<StructureSection load='2aaj' size='340' side='right'caption='[[2aaj]], [[Resolution|resolution]] 2.74&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2aaj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_pavonaceae Pseudomonas pavonaceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AAJ FirstGlance]. <br>
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2AAJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_pavonaceae Pseudomonas pavonaceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAJ 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]] 2.74&#8491;</td></tr>
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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=2aaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aaj OCA], [https://pdbe.org/2aaj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aaj RCSB], [https://www.ebi.ac.uk/pdbsum/2aaj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aaj ProSAT]</span></td></tr>
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==Reference==
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</table>
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Crystal structures of the wild-type, P1A mutant, and inactivated malonate semialdehyde decarboxylase: a structural basis for the decarboxylase and hydratase activities., Almrud JJ, Poelarends GJ, Johnson WH Jr, Serrano H, Hackert ML, Whitman CP, Biochemistry. 2005 Nov 15;44(45):14818-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16274229 16274229]
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== Function ==
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[https://www.uniprot.org/uniprot/Q9EV83_PSEPV Q9EV83_PSEPV]
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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/aa/2aaj_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=2aaj 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: Pseudomonas pavonaceae]]
[[Category: Pseudomonas pavonaceae]]
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[[Category: Single protein]]
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[[Category: Almrud JJ]]
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[[Category: Almrud, J.J.]]
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[[Category: Hackert ML]]
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[[Category: Hackert, M.L.]]
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[[Category: Johnson Jr WH]]
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[[Category: Jr., W.H.Johnson.]]
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[[Category: Poelarends GJ]]
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[[Category: Poelarends, G.J.]]
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[[Category: Serrano H]]
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[[Category: Serrano, H.]]
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[[Category: Whitman CP]]
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[[Category: Whitman, C.P.]]
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[[Category: tautomerase superfamily; beta-alpha-beta; homotrimeric]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:58:10 2008''
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Current revision

Crystal Structures of the Wild-type, Mutant-P1A and Inactivated Malonate Semialdehyde Decarboxylase: A Structural Basis for the Decarboxylase and Hydratase Activities

PDB ID 2aaj

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