2aag: Difference between revisions

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New page: left|200px<br /><applet load="2aag" size="350" color="white" frame="true" align="right" spinBox="true" caption="2aag, resolution 1.85Å" /> '''Crystal Structures o...
 
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[[Image:2aag.gif|left|200px]]<br /><applet load="2aag" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2aag, resolution 1.85&Aring;" />
'''Crystal Structures of the Wild-type, Mutant-P1A and Inactivated Malonate Semialdehyde Decarboxylase: A Structural Basis for the Decarboxylase and Hydratase Activities'''<br />


==Overview==
==Crystal Structures of the Wild-type, Mutant-P1A and Inactivated Malonate Semialdehyde Decarboxylase: A Structural Basis for the Decarboxylase and Hydratase Activities==
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.
<StructureSection load='2aag' size='340' side='right'caption='[[2aag]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
2AAG 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=2AAG OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
 
<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>
==Reference==
</table>
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]
== Function ==
[https://www.uniprot.org/uniprot/Q9EV83_PSEPV Q9EV83_PSEPV]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/2aag_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<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]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:58:08 2008''

Latest revision as of 12:12, 14 February 2024

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

Structural highlights

2aag is a 6 chain structure with sequence from Pseudomonas pavonaceae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9EV83_PSEPV

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

2aag, resolution 1.85Å

Drag the structure with the mouse to rotate

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