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 interactions of the carboxylic acid moiety with the side chain of the, catalytic Glu167 differ. The unique properties of the proline side chain, at position 168 are required to transmit ligand binding to the, conformational change of Glu167: the side chain of Glu167 flips from the, inactive swung-out to the active swung-in conformation on ligand binding, in wild-type TIM, whereas in the mutant this conformational change does, not occur. Further structural comparisons show that in the wild-type, enzyme the concerted movement of loop 6 and loop 7 from unliganded-open to, liganded-closed appears to be facilitated by the interactions of the, phosphate moiety with loop 7. Apparently, the rotation of 90 degrees of, the Gly211-Gly212 peptide plane of loop 7 plays a key role in this, concerted movement.
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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/Triose-phosphate_isomerase Triose-phosphate 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: Triose-phosphate isomerase]]
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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 Mon Nov 5 18:23:33 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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