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[[Image:1mra.gif|left|200px]]<br />
<applet load="1mra" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mra, resolution 2.1&Aring;" />
'''MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE'''<br />


==Overview==
==MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE==
On the basis of the available high-resolution structures of mandelate, racemase (MR) from Pseudomonas putida [Landro, J.A., Gerlt, J.A., Kozarich, J.W., Koo, C.W., Shah, V.J., Kenyon, G.L., Neidhart, D.J., Fujita, J., &amp; Petsko, G.A. (1994) Biochemistry 33, 635-643], Lys 166 and, His 297 are positioned appropriately to participate in catalysis as, acid/base catalysts, with Lys 166 participating as the (S)-specific, acid/base catalyst and His 297 participating as the (R)-specific acid/base, catalyst. The dependence of kcat on pH for the racemization of both (R)-, and (S)-mandelates suggests that the pKaS of the conjugate acids of Lys, 166 and His 297 are both approximately 6.4 [Landro, J.A., Kallarakal, A.T., Ransom, S.C., Gerlt, J.A., Kozarich, J.W., Neidhart, D.J., Kenyon, G.L. (1991) ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8639525 (full description)]]
<StructureSection load='1mra' size='340' side='right'caption='[[1mra]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mra]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MRA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APG:ATROLACTIC+ACID+(2-PHENYL-LACTIC+ACID)'>APG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1mra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mra OCA], [https://pdbe.org/1mra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mra RCSB], [https://www.ebi.ac.uk/pdbsum/1mra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mra ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MANR_PSEPU MANR_PSEPU]
== 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/mr/1mra_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=1mra ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1MRA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]] with MG and APG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Mandelate_racemase Mandelate racemase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.2.2 5.1.2.2]]. Structure known Active Sites: ACT, CAR and MTL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MRA OCA]].
*[[Mandelate racemase|Mandelate racemase]]
 
__TOC__
==Reference==
</StructureSection>
Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant., Schafer SL, Barrett WC, Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL, Biochemistry. 1996 May 7;35(18):5662-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8639525 8639525]
[[Category: Large Structures]]
[[Category: Mandelate racemase]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Clifton JG]]
[[Category: Clifton, J.G.]]
[[Category: Petsko GA]]
[[Category: Petsko, G.A.]]
[[Category: APG]]
[[Category: MG]]
[[Category: atrolactate]]
[[Category: isomerase]]
[[Category: magnesium racemase]]
[[Category: mandelate pathway]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:19:22 2007''

Latest revision as of 07:47, 14 February 2024

MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE

1mra, resolution 2.10Å

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