1nsj

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(New page: 200px<br /><applet load="1nsj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nsj, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1nsj.gif|left|200px]]<br /><applet load="1nsj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nsj, resolution 2.0&Aring;" />
 
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'''CRYSTAL STRUCTURE OF PHOSPHORIBOSYL ANTHRANILATE ISOMERASE FROM THERMOTOGA MARITIMA'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF PHOSPHORIBOSYL ANTHRANILATE ISOMERASE FROM THERMOTOGA MARITIMA==
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The structural basis of thermostability of proteins is of great scientific, and biotechnological interest. Differences in the X-ray structues of, orthologous proteins from hyperthermophilic and mesophilic organisms can, indicate crucial stabilizing interactions. To this end the crystal, structure of dimeric phosphoribosyl anthranilate isomerase from the, hyperthermophile Thermotoga maritima (tPRAI) was determined using phases, derived from the isomorphous replacement method and was refined at 2.0 A, resolution. The comparison to the known 2.0 A structure of PRAI from, Escherichia coli (ePRAI) shows that tPRAI has the complete TIM- or (beta, alpha)8-barrel fold, whereas helix alpha5 in ePRAI is replaced by a loop., The subunits of tPRAI associate via the N-terminal faces of their central, beta-barrels. Two long, symmetry-related loops that protrude reciprocally, into cavities of the other subunit provide for multiple hydrophobic, interactions. Moreover, the side chains of the N-terminal methionines and, the C-terminal leucines of both subunits are immobilized in a hydrophobic, cluster, and the number of salt bridges is increased in tPRAI. These, features appear to be mainly responsible for the high thermostability of, tPRAI. In contrast to other hyperthermostable enzymes, tPRAI at 25 degrees, C is catalytically more efficient than ePRAI, mainly due to its small K(M), value for the substrate [Sterner, R., Kleemann, G. R., Szadkowski, H., Lustig, A., Hennig, M., &amp; Kirschner, K. (1996) Protein Sci. 5, 2000-2008]., The increased number of hydrogen bonds between the phosphate ion and tPRAI, compared to ePRAI could be responsible for this effect.
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<StructureSection load='1nsj' size='340' side='right'caption='[[1nsj]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1nsj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NSJ FirstGlance]. <br>
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1NSJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoribosylanthranilate_isomerase Phosphoribosylanthranilate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.24 5.3.1.24] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NSJ 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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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==Reference==
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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=1nsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsj OCA], [https://pdbe.org/1nsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nsj RCSB], [https://www.ebi.ac.uk/pdbsum/1nsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nsj ProSAT]</span></td></tr>
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Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability., Hennig M, Sterner R, Kirschner K, Jansonius JN, Biochemistry. 1997 May 20;36(20):6009-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9166771 9166771]
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</table>
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[[Category: Phosphoribosylanthranilate isomerase]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/TRPF_THEMA TRPF_THEMA]
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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/ns/1nsj_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=1nsj 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: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Hennig, M.]]
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[[Category: Hennig M]]
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[[Category: Jansonius, J.N.J.]]
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[[Category: Jansonius JNJ]]
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[[Category: PO4]]
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[[Category: isomerase]]
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[[Category: phosphoribosyl anthranilate isomerase]]
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[[Category: thermostability]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:31:28 2007''
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Current revision

CRYSTAL STRUCTURE OF PHOSPHORIBOSYL ANTHRANILATE ISOMERASE FROM THERMOTOGA MARITIMA

PDB ID 1nsj

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