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| [[Image:2aag.gif|left|200px]]
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| {{Structure
| | ==Crystal Structures of the Wild-type, Mutant-P1A and Inactivated Malonate Semialdehyde Decarboxylase: A Structural Basis for the Decarboxylase and Hydratase Activities== |
| |PDB= 2aag |SIZE=350|CAPTION= <scene name='initialview01'>2aag</scene>, resolution 1.85Å
| | <StructureSection load='2aag' size='340' side='right'caption='[[2aag]], [[Resolution|resolution]] 1.85Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND=
| | <table><tr><td colspan='2'>[[2aag]] is a 6 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=2AAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AAG FirstGlance]. <br> |
| |ACTIVITY=
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| |GENE= orf130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=47881 Pseudomonas pavonaceae])
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2aag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aag OCA], [https://pdbe.org/2aag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aag RCSB], [https://www.ebi.ac.uk/pdbsum/2aag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aag ProSAT]</span></td></tr> |
| }}
| | </table> |
| | | == Function == |
| '''Crystal Structures of the Wild-type, Mutant-P1A and Inactivated Malonate Semialdehyde Decarboxylase: A Structural Basis for the Decarboxylase and Hydratase Activities'''
| | [https://www.uniprot.org/uniprot/Q9EV83_PSEPV Q9EV83_PSEPV] |
| | | == Evolutionary Conservation == |
| | | [[Image:Consurf_key_small.gif|200px|right]] |
| ==Overview== | | Check<jmol> |
| 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.
| | <jmolCheckbox> |
| | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/2aag_consurf.spt"</scriptWhenChecked> |
| ==About this Structure== | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| 2AAG is a [[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=2AAG OCA].
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | | </jmolCheckbox> |
| ==Reference== | | </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=2aag ConSurf]. |
| 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://www.ncbi.nlm.nih.gov/pubmed/16274229 16274229]
| | <div style="clear:both"></div> |
| | __TOC__ |
| | </StructureSection> |
| | [[Category: Large Structures]] |
| [[Category: Pseudomonas pavonaceae]] | | [[Category: Pseudomonas pavonaceae]] |
| [[Category: Single protein]]
| | [[Category: Almrud JJ]] |
| [[Category: Almrud, J J.]] | | [[Category: Hackert ML]] |
| [[Category: Hackert, M L.]] | | [[Category: Johnson Jr WH]] |
| [[Category: Jr., W H.Johnson.]] | | [[Category: Poelarends GJ]] |
| [[Category: Poelarends, G J.]] | | [[Category: Serrano H]] |
| [[Category: Serrano, H.]] | | [[Category: Whitman CP]] |
| [[Category: Whitman, C P.]] | |
| [[Category: tautomerase superfamily; beta-alpha-beta; homotrimeric]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:47:22 2008''
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