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2j27

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[[Image:2j27.gif|left|200px]]<br />
 
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<applet load="2j27" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2j27, resolution 1.15&Aring;" />
 
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'''THE FUNCTIONAL ROLE OF THE CONSERVED ACTIVE SITE PROLINE OF TRIOSEPHOSPHATE ISOMERASE'''<br />
 
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==Overview==
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==The functional role of the conserved active site proline of triosephosphate isomerase==
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The importance of the fully conserved active site proline, Pro168, for the, reaction mechanism of triosephosphate isomerase (TIM) has been, investigated by studying the enzymatic and crystallographic properties of, the P168A variant of trypanosomal TIM. In TIM, Pro168 follows the key, catalytic residue Glu167, situated at the beginning of the flexible active, site loop (loop 6). Turnover numbers of the P168A variant for its, substrates are reduced approximately 50-fold, whereas the Km values are, approximately 2 times lower. The affinity of the P168A variant for the, transition state analogue 2-phosphoglycolate (2PG) is reduced 5-fold. The, crystal structures of unliganded and liganded (2PG) P168A show that the, phosphate moiety of 2PG is bound similarly as in wild-type TIM, whereas, the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?17176070 (full description)]]
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<StructureSection load='2j27' size='340' side='right'caption='[[2j27]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2j27]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J27 FirstGlance]. <br>
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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]] 1.15&#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=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2j27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j27 OCA], [https://pdbe.org/2j27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j27 RCSB], [https://www.ebi.ac.uk/pdbsum/2j27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j27 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TPIS_TRYBB TPIS_TRYBB]
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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/j2/2j27_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=2j27 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2J27 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]] with PGA and SO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Isomerase Isomerase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J27 OCA]].
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*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase(,)., Casteleijn MG, Alahuhta M, Groebel K, El-Sayed I, Augustyns K, Lambeir AM, Neubauer P, Wierenga RK, Biochemistry. 2006 Dec 26;45(51):15483-15494. Epub 2006 Dec 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17176070 17176070]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Trypanosoma brucei brucei]]
[[Category: Trypanosoma brucei brucei]]
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[[Category: Alahuhta, M.]]
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[[Category: Alahuhta M]]
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[[Category: Augustyns, K.]]
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[[Category: Augustyns K]]
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[[Category: Casteleijn, M.G.]]
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[[Category: Casteleijn MG]]
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[[Category: El-Sayed, I.]]
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[[Category: El-Sayed I]]
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[[Category: Groebel, K.]]
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[[Category: Groebel K]]
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[[Category: Lambeir, A.M.]]
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[[Category: Lambeir AM]]
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[[Category: Neubauer, P.]]
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[[Category: Neubauer P]]
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[[Category: Wierenga, R.K.]]
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[[Category: Wierenga RK]]
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[[Category: PGA]]
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[[Category: SO4]]
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[[Category: 2-phospho glycolate]]
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[[Category: 2pg]]
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[[Category: atomic resolution]]
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[[Category: fatty acid biosynthesis]]
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[[Category: gluconeogenesis]]
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[[Category: glycolysis]]
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[[Category: glycosome]]
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[[Category: isomerase]]
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[[Category: lipid synthesis]]
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[[Category: loop7]]
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[[Category: pentose shunt]]
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[[Category: point mutation]]
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[[Category: protein engineering]]
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[[Category: tim]]
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[[Category: tim-barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:30:36 2007''
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Current revision

The functional role of the conserved active site proline of triosephosphate isomerase

PDB ID 2j27

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