1bqg

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(New page: 200px<br /><applet load="1bqg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bqg, resolution 2.3&Aring;" /> '''THE STRUCTURE OF THE ...)
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[[Image:1bqg.jpg|left|200px]]<br /><applet load="1bqg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bqg, resolution 2.3&Aring;" />
 
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'''THE STRUCTURE OF THE D-GLUCARATE DEHYDRATASE PROTEIN FROM PSEUDOMONAS PUTIDA'''<br />
 
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==Overview==
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==THE STRUCTURE OF THE D-GLUCARATE DEHYDRATASE PROTEIN FROM PSEUDOMONAS PUTIDA==
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The structure of (D)-glucarate dehydratase from Pseudomonas putida (GlucD), has been solved at 2.3 A resolution by multiple isomorphous replacement, and refined to a final R-factor of 19.0%. The protein crystallizes in the, space group I222 with one subunit in the asymmetric unit. The unit cell, dimensions are a = 69.6 A, b = 108.8 A, and c = 122.6 A. The crystals were, grown using the batch method where the primary precipitant was, poly(ethylene glycol) 1000. The structure reveals that GlucD is a tetramer, of four identical polypeptides, each containing 451 residues. The, structure was determined without a bound substrate or substrate analogue., Three disordered regions are noted: the N-terminus through residue 11, a, loop containing residues 99 through 110, and the C-terminus from residue, 423. On the basis of primary sequence alignments, we previously concluded, that GlucD is a member of the mandelate racemase (MR) subfamily of the, enolase superfamily [Babbitt, P. C., Hasson, M. S., Wedekind, J. E., Palmer, D. R. J., Barrett, W. C., Reed, G. J., Rayment, I., Ringe, D., Kenyon, G. L., and Gerlt, J. A. (1996) Biochemistry 35, 16489-16501]. This, prediction is now verified, since the overall fold of GlucD is strikingly, similar to those of MR, muconate lactonizing enzyme I, and enolase. Also, many of the active site residues of GlucD can be superimposed on those, found in the active site of MR. The implications of this structure on the, evolution of catalysis in the enolase superfamily are discussed.
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<StructureSection load='1bqg' size='340' side='right'caption='[[1bqg]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1bqg]] 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=1BQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BQG FirstGlance]. <br>
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1BQG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Active as [http://en.wikipedia.org/wiki/Glucarate_dehydratase Glucarate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.40 4.2.1.40] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BQG 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]] 2.3&#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=1bqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bqg OCA], [https://pdbe.org/1bqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bqg RCSB], [https://www.ebi.ac.uk/pdbsum/1bqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bqg ProSAT]</span></td></tr>
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==Reference==
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</table>
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Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putida., Gulick AM, Palmer DR, Babbitt PC, Gerlt JA, Rayment I, Biochemistry. 1998 Oct 13;37(41):14358-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9772161 9772161]
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== Function ==
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[[Category: Glucarate dehydratase]]
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[https://www.uniprot.org/uniprot/GUDD_PSEPU GUDD_PSEPU] Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc).
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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/bq/1bqg_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=1bqg 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 putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Babbitt PC]]
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[[Category: Babbitt, P.C.]]
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[[Category: Gerlt JA]]
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[[Category: Gerlt, J.A.]]
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[[Category: Gulick AM]]
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[[Category: Gulick, A.M.]]
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[[Category: Palmer DRJ]]
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[[Category: Palmer, D.R.J.]]
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[[Category: Rayment I]]
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[[Category: Rayment, I.]]
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[[Category: enolase superfamily]]
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[[Category: glucarate]]
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[[Category: tim barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:50:18 2007''
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Current revision

THE STRUCTURE OF THE D-GLUCARATE DEHYDRATASE PROTEIN FROM PSEUDOMONAS PUTIDA

PDB ID 1bqg

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