2j27

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|PDB= 2j27 |SIZE=350|CAPTION= <scene name='initialview01'>2j27</scene>, resolution 1.15&Aring;
|PDB= 2j27 |SIZE=350|CAPTION= <scene name='initialview01'>2j27</scene>, resolution 1.15&Aring;
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|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]
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|ACTIVITY= <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>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j27 OCA], [http://www.ebi.ac.uk/pdbsum/2j27 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j27 RCSB]</span>
}}
}}
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[[Category: Neubauer, P.]]
[[Category: Neubauer, P.]]
[[Category: Wierenga, R K.]]
[[Category: Wierenga, R K.]]
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[[Category: PGA]]
 
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[[Category: SO4]]
 
[[Category: 2-phospho glycolate]]
[[Category: 2-phospho glycolate]]
[[Category: 2pg]]
[[Category: 2pg]]
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[[Category: tim-barrel]]
[[Category: tim-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:36:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:52:02 2008''

Revision as of 00:52, 31 March 2008

Image:2j27.jpg


PDB ID 2j27

Drag the structure with the mouse to rotate
, resolution 1.15Å
Sites:
Ligands: ,
Activity: Triose-phosphate isomerase, with EC number 5.3.1.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



THE FUNCTIONAL ROLE OF THE CONSERVED ACTIVE SITE PROLINE OF TRIOSEPHOSPHATE ISOMERASE


Overview

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.

About this Structure

2J27 is a Single protein structure of sequence from Trypanosoma brucei brucei. Full crystallographic information is available from OCA.

Reference

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):15483-94. Epub 2006 Dec 19. PMID:17176070

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