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<StructureSection load='1tpv' size='340' side='right'caption='[[1tpv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1tpv' size='340' side='right'caption='[[1tpv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1tpv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TPV FirstGlance]. <br>
<table><tr><td colspan='2'>[[1tpv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TPV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGH:PHOSPHOGLYCOLOHYDROXAMIC+ACID'>PGH</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGH:PHOSPHOGLYCOLOHYDROXAMIC+ACID'>PGH</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tpv OCA], [http://pdbe.org/1tpv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tpv RCSB], [http://www.ebi.ac.uk/pdbsum/1tpv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tpv ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tpv OCA], [https://pdbe.org/1tpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tpv RCSB], [https://www.ebi.ac.uk/pdbsum/1tpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tpv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPIS_CHICK TPIS_CHICK]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1tpv ConSurf].
</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=1tpv ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structural basis for the 3000-fold decrease in catalytic efficiency of the H95N mutant chicken triosephosphate isomerase and the 60-fold regain of catalytic efficiency in the double mutant, H95N.S96P, have been analyzed. The results from a combination of X-ray crystallography and Fourier transform infrared spectroscopy experiments indicate that the predominant defect in the H95N mutant isomerase appears to be its inability to bind the substrate in a coplanar, cis conformation. The structures of each mutant isomerase were determined from X-ray crystallography of the complex of phosphoglycolohydroxamate (PGH), an intermediate analog with the isomerase, and each was solved to a resolution of 1.9 A. The PGH appeared to be in two different conformations in which the enediol-mimicking atoms, O2-N2-C1-O1, of the PGH were not coplanar. No density was observed that would correspond to the coplanar conformation. Two bands are observed for the dihydroxyacetone phosphate carbonyl in the H95N mutant FTIR spectrum, and these can be explained if the O1 of DHAP, like the O1 of PGH in the crystal structure, is in two different positions. Two ordered water molecules are located between O1 of PGH and N delta of N95. Comparison of the structure of the pseudorevertant, H95N.S96P with that for the H95N single mutant, shows that S96P mutation causes the double mutant to regain the ability to bind PGH predominantly in the coplanar, cis conformation. Electron density for a single ordered water molecule bridging the N95 amide side chain and the O2 of PGH is observed, but the density was weak, perhaps indicating that the water molecule is somewhat disordered. Whether or not a water molecule is hydrogen bonded to O2 of PGH may explain the two carbonyl stretching frequencies observed for the GAP carbonyl. Together, the crystal structures and the FTIR data allow a complete explanation of the catalytic properties of these two mutant isomerases.
The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase.,Komives EA, Lougheed JC, Zhang Z, Sugio S, Narayana N, Xuong NH, Petsko GA, Ringe D Biochemistry. 1996 Dec 3;35(48):15474-84. PMID:8952501<ref>PMID:8952501</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tpv" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Triose Phosphate Isomerase|Triose Phosphate Isomerase]]
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chick]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Triose-phosphate isomerase]]
[[Category: Knowles JR]]
[[Category: Knowles, J R]]
[[Category: Komives EA]]
[[Category: Komives, E A]]
[[Category: Liu KD]]
[[Category: Liu, K D]]
[[Category: Narayana N]]
[[Category: Narayana, N]]
[[Category: Petsko GA]]
[[Category: Petsko, G A]]
[[Category: Ringe D]]
[[Category: Ringe, D]]
[[Category: Stock AM]]
[[Category: Stock, A M]]
[[Category: Sugio S]]
[[Category: Sugio, S]]
[[Category: Xuong NgH]]
[[Category: Xuong, Ng H]]
[[Category: Zhang Z]]
[[Category: Zhang, Z]]

Latest revision as of 11:41, 14 February 2024

S96P CHANGE IS A SECOND-SITE SUPPRESSOR FOR H95N SLUGGISH MUTANT TRIOSEPHOSPHATE ISOMERASES96P CHANGE IS A SECOND-SITE SUPPRESSOR FOR H95N SLUGGISH MUTANT TRIOSEPHOSPHATE ISOMERASE

Structural highlights

1tpv is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TPIS_CHICK

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1tpv, resolution 1.90Å

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