1tpf
From Proteopedia
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| - | [[Image:1tpf.gif|left|200px]] | + | [[Image:1tpf.gif|left|200px]] |
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| - | '''COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS''' | + | {{Structure |
| + | |PDB= 1tpf |SIZE=350|CAPTION= <scene name='initialview01'>1tpf</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=DMS:DIMETHYL SULFOXIDE'>DMS</scene> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TPF is a [ | + | 1TPF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TPF OCA]. |
==Reference== | ==Reference== | ||
| - | Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms., Kishan KV, Zeelen JP, Noble ME, Borchert TV, Wierenga RK, Protein Sci. 1994 May;3(5):779-87. PMID:[http:// | + | Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms., Kishan KV, Zeelen JP, Noble ME, Borchert TV, Wierenga RK, Protein Sci. 1994 May;3(5):779-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8061607 8061607] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Triose-phosphate isomerase]] | [[Category: Triose-phosphate isomerase]] | ||
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[[Category: isomerase(intramolecular oxidoreductase)]] | [[Category: isomerase(intramolecular oxidoreductase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:21:28 2008'' |
Revision as of 12:21, 20 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | |||||||
| Activity: | Triose-phosphate isomerase, with EC number 5.3.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS
Overview
Triosephosphate isomerase (TIM) is a dimeric enzyme consisting of 2 identical subunits. Trypanosomal TIM can be crystallized in 4 different spacegroups: P2(1)2(1)2(1), C2(big cell), C2(small cell), and P1. The P1 crystal form only grows in the presence of 1.4 M DMSO; there are 2 DMSO binding sites per subunit. The structures have been refined at a resolution of 1.83 A, 2.10 A, 2.13 A, and 1.80 A, respectively. In the 4 different spacegroups the TIM subunit can be observed in the context of 7 different crystallographic environments. In the C2 cells, the dimer 2-fold axis coincides with a crystallographic 2-fold axis. The similarities and differences of the 7 subunits are discussed. In 6 subunits the flexible loop (loop 6) is open, whereas in the P2(1)2(1)2(1) cell, the flexible loop of subunit 2 is in an almost closed conformation. The crystal contacts in the 4 different crystal forms are predominantly generated by polar residues in loops. A statistical analysis of the residues involved in crystal contacts shows that, in particular, serines are frequently involved in these interactions; 19% of the exposed serines are involved in crystal contacts.
About this Structure
1TPF is a Single protein structure of sequence from Trypanosoma brucei brucei. Full crystallographic information is available from OCA.
Reference
Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms., Kishan KV, Zeelen JP, Noble ME, Borchert TV, Wierenga RK, Protein Sci. 1994 May;3(5):779-87. PMID:8061607
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