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1tpd

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[[Image:1tpd.gif|left|200px]]
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{{STRUCTURE_1tpd| PDB=1tpd | SCENE= }}
{{STRUCTURE_1tpd| PDB=1tpd | SCENE= }}
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'''STRUCTURES OF THE "OPEN" AND "CLOSED" STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM'''
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===STRUCTURES OF THE "OPEN" AND "CLOSED" STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM===
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==Overview==
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The structure of trypanosomal triosephosphate isomerase (TIM) has been solved at a resolution of 2.1A in a new crystal form grown at pH 8.8 from PEG6000. In this new crystal form (space group C2, cell dimensions 94.8 A, 48.3 A, 131.0 A, 90.0 degrees, 100.3 degrees, 90.0 degrees), TIM is present in a ligand-free state. The asymmetric unit consists of two TIM subunits. Each of these subunits is part of a dimer which is sitting on a crystallographic twofold axis, such that the crystal packing is formed from two TIM dimers in two distinct environments. The two constituent monomers of a given dimer are, therefore, crystallographically equivalent. In the ligand-free state of TIM in this crystal form, the two types of dimer are very similar in structure, with the flexible loops in the "open" conformation. For one dimer (termed molecule-1), the flexible loop (loop-6) is involved in crystal contacts. Crystals of this type have been used in soaking experiments with 0.4 M ammonium sulphate (studied at 2.4 A resolution), and with 40 microM phosphoglycolohydroxamate (studied at 2.5 A resolution). It is found that transfer to 0.4 M ammonium sulphate (equal to 80 times the Ki of sulphate for TIM), gives rise to significant sulphate binding at the active site of one dimer (termed molecule-2), and less significant binding at the active site of the other. In neither dimer does sulphate induce a "closed" conformation. In a mother liquor containing 40 microM phosphoglycolohydroxamate (equal to 10 times the Ki of phosphoglycolohydroxamate for TIM), an inhibitor molecule binds at the active site of only that dimer of which the flexible loop is free from crystal contacts (molecule-2). In this dimer, it induces a closed conformation. These three structures are compared and discussed with respect to the mode of binding of ligand in the active site as well as with respect to the conformational changes resulting from ligand binding.
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(as it appears on PubMed at http://www.pubmed.gov), where 8356028 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8356028}}
==About this Structure==
==About this Structure==
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[[Category: Wierenga, R K.]]
[[Category: Wierenga, R K.]]
[[Category: Zeelen, J Ph.]]
[[Category: Zeelen, J Ph.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:13:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:26:23 2008''

Revision as of 13:26, 27 July 2008

Image:1tpd.png

Template:STRUCTURE 1tpd

STRUCTURES OF THE "OPEN" AND "CLOSED" STATE OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE, AS OBSERVED IN A NEW CRYSTAL FORM: IMPLICATIONS FOR THE REACTION MECHANISM

Template:ABSTRACT PUBMED 8356028

About this Structure

1TPD is a Single protein structure of sequence from Trypanosoma brucei brucei. Full crystallographic information is available from OCA.

Reference

Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism., Noble ME, Zeelen JP, Wierenga RK, Proteins. 1993 Aug;16(4):311-26. PMID:8356028

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