4bi7: Difference between revisions

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<StructureSection load='4bi7' size='340' side='right'caption='[[4bi7]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='4bi7' size='340' side='right'caption='[[4bi7]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4bi7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Giain Giain]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2yc7 2yc7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BI7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4bi7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Giardia_intestinalis Giardia intestinalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2yc7 2yc7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BI7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BI7 FirstGlance]. <br>
</td></tr><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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4bi5|4bi5]], [[4bi6|4bi6]]</div></td></tr>
<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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=4bi7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bi7 OCA], [https://pdbe.org/4bi7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bi7 RCSB], [https://www.ebi.ac.uk/pdbsum/4bi7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bi7 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=4bi7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bi7 OCA], [https://pdbe.org/4bi7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bi7 RCSB], [https://www.ebi.ac.uk/pdbsum/4bi7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bi7 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/TPI1_GIAIN TPI1_GIAIN]
BACKGROUND: We have previously proposed triosephosphate isomerase of Giardia lamblia (GlTIM) as a target for rational drug design against giardiasis, one of the most common parasitic infections in humans. Since the enzyme exists in the parasite and the host, selective inhibition is a major challenge because essential regions that could be considered molecular targets are highly conserved. Previous biochemical evidence showed that chemical modification of the non-conserved non-catalytic cysteine 222 (C222) inactivates specifically GlTIM. The inactivation correlates with the physicochemical properties of the modifying agent: addition of a non-polar, small chemical group at C222 reduces the enzyme activity by one half, whereas negatively charged, large chemical groups cause full inactivation. RESULTS: In this work we used mutagenesis to extend our understanding of the functional and structural effects triggered by modification of C222. To this end, six GlTIM C222 mutants with side chains having diverse physicochemical characteristics were characterized. We found that the polarity, charge and volume of the side chain in the mutant amino acid differentially alter the activity, the affinity, the stability and the structure of the enzyme. The data show that mutagenesis of C222 mimics the effects of chemical modification. The crystallographic structure of C222D GlTIM shows the disruptive effects of introducing a negative charge at position 222: the mutation perturbs loop 7, a region of the enzyme whose interactions with the catalytic loop 6 are essential for TIM stability, ligand binding and catalysis. The amino acid sequence of TIM in phylogenetic diverse groups indicates that C222 and its surrounding residues are poorly conserved, supporting the proposal that this region is a good target for specific drug design. CONCLUSIONS: The results demonstrate that it is possible to inhibit species-specifically a ubiquitous, structurally highly conserved enzyme by modification of a non-conserved, non-catalytic residue through long-range perturbation of essential regions.
 
Structural and Functional Perturbation of Giardia lamblia Triosephosphate Isomerase by Modification of a Non-Catalytic, Non-Conserved Region.,Hernandez-Alcantara G, Torres-Larios A, Enriquez-Flores S, Garcia-Torres I, Castillo-Villanueva A, Mendez ST, de la Mora-de la Mora I, Gomez-Manzo S, Torres-Arroyo A, Lopez-Velazquez G, Reyes-Vivas H, Oria-Hernandez J PLoS One. 2013 Jul 22;8(7):e69031. doi: 10.1371/journal.pone.0069031. Print 2013. PMID:23894402<ref>PMID:23894402</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bi7" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
*[[Triose phosphate isomerase 3D structures|Triose phosphate isomerase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Giain]]
[[Category: Giardia intestinalis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Triose-phosphate isomerase]]
[[Category: Enriquez-Flores S]]
[[Category: Enriquez-Flores, S]]
[[Category: Hernandez-Alcantara G]]
[[Category: Hernandez-Alcantara, G]]
[[Category: Oria-Hernandez J]]
[[Category: Oria-Hernandez, J]]
[[Category: Reyes-Vivas H]]
[[Category: Reyes-Vivas, H]]
[[Category: Torres-Larios A]]
[[Category: Torres-Larios, A]]
[[Category: Isomerase]]

Latest revision as of 10:17, 1 May 2024

CRYSTAL STRUCTURE OF A MUTANT (C202A) OF TRIOSEPHOSPHATE ISOMERASE FROM GIARDIA LAMBLIA. COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACIDCRYSTAL STRUCTURE OF A MUTANT (C202A) OF TRIOSEPHOSPHATE ISOMERASE FROM GIARDIA LAMBLIA. COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID

Structural highlights

4bi7 is a 1 chain structure with sequence from Giardia intestinalis. This structure supersedes the now removed PDB entry 2yc7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TPI1_GIAIN

See Also

4bi7, resolution 1.60Å

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