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1kra

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[[Image:1kra.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF KLEBSIELLA AEROGENES UREASE, ITS APOENZYME AND TWO ACTIVE SITE MUTANTS==
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|PDB= 1kra |SIZE=350|CAPTION= <scene name='initialview01'>1kra</scene>, resolution 2.3&Aring;
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<StructureSection load='1kra' size='340' side='right'caption='[[1kra]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1kra]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3kau 3kau]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KRA FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Urease Urease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.5 3.5.1.5]
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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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|GENE=
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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=1kra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kra OCA], [https://pdbe.org/1kra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kra RCSB], [https://www.ebi.ac.uk/pdbsum/1kra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kra ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/URE3_KLEAE URE3_KLEAE]
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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/kr/1kra_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=1kra ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF KLEBSIELLA AEROGENES UREASE, ITS APOENZYME AND TWO ACTIVE SITE MUTANTS'''
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==See Also==
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*[[Urease 3D structures|Urease 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Urease from Klebsiella aerogenes [Jabri et al. (1995) Science 268, 998-1004] is an (alpha beta gamma)3 trimer with each alpha-subunit having an (alpha beta)8-barrel domain containing a binickel active center. Here we examine structure-function relations for urease in more detail through structural analysis of the urease apoenzyme at 2.3 A resolution and mutants of two key catalytic residues (H219A and H320A) at 2.5 A resolution. With the exception of the active site, in which a water molecule takes the place of the missing carbamate and nickel atoms, the structure of the apoenzyme is nearly identical to that of the holoenzyme, suggesting a high degree of preorganization which helps explain the tight binding of nickel. In the structure of H219A, the major change involves a conformational shift and ordering of the active site flap, but a small shift in the side chain of Asp alpha 221 could contribute to the lower activity of H219A. In the H320A structure, the catalytic water, primarily a Ni-2 ligand in the holoenzyme, shifts into a bridging position. This shift shows that the nickel ligation is rather sensitive to the environment and the change in ligation may contribute to the 10(5)-fold lower activity of H320A. In addition, these results show that urease is resilient to the loss of nickel ions and mutations. Analysis of the urease tertiary/quaternary structure suggests that the stability of this enzyme may be largely due to its burial of an unusually large fraction of its residues: 50% in the gamma-subunit, 30% in the beta-subunit, and 60% in the alpha-subunit.
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==About this Structure==
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1KRA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. This structure supersedes the now removed PDB entry 3KAU. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRA OCA].
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==Reference==
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Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants., Jabri E, Karplus PA, Biochemistry. 1996 Aug 20;35(33):10616-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8718850 8718850]
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[[Category: Klebsiella aerogenes]]
[[Category: Klebsiella aerogenes]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Urease]]
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[[Category: Jabri E]]
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[[Category: Jabri, E.]]
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[[Category: Karplus PA]]
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[[Category: Karplus, P A.]]
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[[Category: apoenzyme]]
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[[Category: nickel metalloenzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:21:09 2008''
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Current revision

CRYSTAL STRUCTURE OF KLEBSIELLA AEROGENES UREASE, ITS APOENZYME AND TWO ACTIVE SITE MUTANTS

PDB ID 1kra

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