1tmh: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1tmh.gif|left|200px]]


{{Structure
==MODULAR MUTAGENESIS OF A TIM-BARREL ENZYME: THE CRYSTAL STRUCTURE OF A CHIMERIC E. COLI TIM HAVING THE EIGHTH (BETA-ALPHA)-UNIT REPLACED BY THE EQUIVALENT UNIT OF CHICKEN TIM==
|PDB= 1tmh |SIZE=350|CAPTION= <scene name='initialview01'>1tmh</scene>, resolution 2.8&Aring;
<StructureSection load='1tmh' size='340' side='right'caption='[[1tmh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
<table><tr><td colspan='2'>[[1tmh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TMH FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1tmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tmh OCA], [https://pdbe.org/1tmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tmh RCSB], [https://www.ebi.ac.uk/pdbsum/1tmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tmh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPIS_ECOLI TPIS_ECOLI] [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/tm/1tmh_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=1tmh ConSurf].
<div style="clear:both"></div>


'''MODULAR MUTAGENESIS OF A TIM-BARREL ENZYME: THE CRYSTAL STRUCTURE OF A CHIMERIC E. COLI TIM HAVING THE EIGHTH (BETA-ALPHA)-UNIT REPLACED BY THE EQUIVALENT UNIT OF CHICKEN TIM'''
==See Also==
 
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The crystal structure of a hybrid Escherichia coli triosephosphate isomerase (TIM) has been determined at 2.8 A resolution. The hybrid TIM (ETIM8CHI) was constructed by replacing the eighth beta alpha-unit of E. coli TIM with the equivalent unit of chicken TIM. This replacement involves 10 sequence changes. One of the changes concerns the mutation of a buried alanine (Ala232 in strand 8) into a phenylalanine. The ETIM8CHI structure shows that the A232F sequence change can be incorporated by a side-chain rotation of Phe224 (in helix 7). No cavities or strained dihedrals are observed in ETIM8CHI in the region near position 232, which is in agreement with the observation that ETIM8CHI and E.coli TIM have similar stabilities. The largest CA (C-alpha atom) movements, approximately 3 A, are seen for the C-terminal end of helix 8 (associated with the outward rotation of Phe224) and for the residues in the loop after helix 1 (associated with sequence changes in helix 8). From the structure it is not clear why the kcat of ETIM8CHI is 10 times lower than in wild type E.coli TIM.
 
==About this Structure==
1TMH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TMH OCA].
 
==Reference==
Modular mutagenesis of a TIM-barrel enzyme: the crystal structure of a chimeric E. coli TIM having the eighth beta alpha-unit replaced by the equivalent unit of chicken TIM., Kishan R, Zeelen JP, Noble ME, Borchert TV, Mainfroid V, Goraj K, Martial JA, Wierenga RK, Protein Eng. 1994 Aug;7(8):945-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7809033 7809033]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Triose-phosphate isomerase]]
[[Category: Radha Kishan KV]]
[[Category: Kishan, K V.Radha.]]
[[Category: Wierenga RK]]
[[Category: Wierenga, R K.]]
[[Category: Zeelen JPh]]
[[Category: Zeelen, J Ph.]]
[[Category: SO4]]
[[Category: isomerase(intramolecular oxidoreductase)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:20:20 2008''

Latest revision as of 11:40, 14 February 2024

MODULAR MUTAGENESIS OF A TIM-BARREL ENZYME: THE CRYSTAL STRUCTURE OF A CHIMERIC E. COLI TIM HAVING THE EIGHTH (BETA-ALPHA)-UNIT REPLACED BY THE EQUIVALENT UNIT OF CHICKEN TIMMODULAR MUTAGENESIS OF A TIM-BARREL ENZYME: THE CRYSTAL STRUCTURE OF A CHIMERIC E. COLI TIM HAVING THE EIGHTH (BETA-ALPHA)-UNIT REPLACED BY THE EQUIVALENT UNIT OF CHICKEN TIM

Structural highlights

1tmh is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TPIS_ECOLI 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

1tmh, resolution 2.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1tmh&oldid=4055604"