1tph: Difference between revisions

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New page: left|200px<br /><applet load="1tph" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tph, resolution 1.8Å" /> '''1.8 ANGSTROMS CRYSTAL...
 
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[[Image:1tph.gif|left|200px]]<br /><applet load="1tph" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1tph, resolution 1.8&Aring;" />
'''1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE CHICKEN TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX'''<br />


==Overview==
==1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE CHICKEN TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX==
The crystal structure of recombinant chicken triosephosphate isomerase, (TIM, E.C. 5.3.1.1) complexed with the intermediate analogue, phosphoglycolohydroxamate (PGH) has been solved by the method of molecular, replacement and refined to an R-factor of 18.5% at 1.8-A resolution. The, structure is essentially identical to that of the yeast TIM-PGH complex, [Davenport, R. C., et al. (1991) Biochemistry 30, 5821-5826] determined, earlier and refined at comparable resolution. This identity extends to the, high-energy conformations of the active-site residues Lys13 and Ser211, as, well as the positions of several bound water molecules that are retained, in the active site when PGH is bound. Comparison with the structure of, uncomplexed chicken TIM shows that the catalytic base, Glu165, moves, several angstroms when PGH binds. This movement may provide a trigger for, a larger conformational change, one of 7 A, in a loop near the active, site, which folds down like a lid to shield the bound inhibitor and, catalytic residues from contact with bulk solvent. These same, conformational changes were seen in crystalline yeast TIM upon binding of, PGH; their occurrence here in a different crystal form of TIM eliminates, the possibility that they are an artifact of crystal packing.
<StructureSection load='1tph' size='340' side='right'caption='[[1tph]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tph]] 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=1TPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TPH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=1tph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tph OCA], [https://pdbe.org/1tph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tph RCSB], [https://www.ebi.ac.uk/pdbsum/1tph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tph ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPIS_CHICK TPIS_CHICK]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tp/1tph_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1tph ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1TPH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with PGH as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TPH OCA].
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution., Zhang Z, Sugio S, Komives EA, Liu KD, Knowles JR, Petsko GA, Ringe D, Biochemistry. 1994 Mar 15;33(10):2830-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8130195 8130195]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[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: Petsko GA]]
[[Category: Petsko, G.A.]]
[[Category: Ringe D]]
[[Category: Ringe, D.]]
[[Category: Sugio S]]
[[Category: Sugio, S.]]
[[Category: Zhang Z]]
[[Category: Zhang, Z.]]
[[Category: PGH]]
[[Category: triosephosphate isomerase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:29:17 2007''

Latest revision as of 11:41, 14 February 2024

1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE CHICKEN TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE CHICKEN TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX

Structural highlights

1tph 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 1.8Å
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

1tph, resolution 1.80Å

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