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1fs5

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[[Image:1fs5.gif|left|200px]]
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{{STRUCTURE_1fs5| PDB=1fs5 | SCENE= }}
{{STRUCTURE_1fs5| PDB=1fs5 | SCENE= }}
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'''A DISCOVERY OF THREE ALTERNATE CONFORMATIONS IN THE ACTIVE SITE OF GLUCOSAMINE-6-PHOSPHATE ISOMERASE'''
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===A DISCOVERY OF THREE ALTERNATE CONFORMATIONS IN THE ACTIVE SITE OF GLUCOSAMINE-6-PHOSPHATE ISOMERASE===
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==Overview==
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A new crystallographic structure of the free active-site R conformer of the allosteric enzyme glucosamine-6-phosphate deaminase from Escherichia coli, coupled with previously reported structures of the T and R conformers, generates a detailed description of the heterotropic allosteric transition in which structural flexibility plays a central role. The T conformer's external zone [Horjales et al. (1999), Structure, 7, 527-536] presents higher B values than in the R conformers. The ligand-free enzyme (T conformer) undergoes an allosteric transition to the free active-site R conformer upon binding of the allosteric activator. This structure shows three alternate conformations of the mobile section of the active-site lid (residues 163-182), in comparison to the high B values for the unique conformation of the T conformer. One of these alternate R conformations corresponds to the active-site lid found when the substrate is bound. The disorder associated with the three alternate conformations can be related to the biological regulation of the K(m) of the enzyme for the reaction, which is metabolically required to maintain adequate concentrations of the activator, which holds the enzyme in its R state. Seven alternate conformations for the active-site lid and three for the C-terminus were refined for the T structure using isotropic B factors. Some of these conformers approach that of the R conformer in geometry. Furthermore, the direction of the atomic vibrations obtained with anisotropic B refinement supports the hypothesis of an oscillating rather than a tense T state. The concerted character of the allosteric transition is also analysed in view of the apparent dynamics of the conformers.
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(as it appears on PubMed at http://www.pubmed.gov), where 11752775 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11752775}}
==About this Structure==
==About this Structure==
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[[Category: Entropic effect]]
[[Category: Entropic effect]]
[[Category: Multiple conformer]]
[[Category: Multiple conformer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:42:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:51:47 2008''

Revision as of 00:51, 1 July 2008

Image:1fs5.png

Template:STRUCTURE 1fs5

A DISCOVERY OF THREE ALTERNATE CONFORMATIONS IN THE ACTIVE SITE OF GLUCOSAMINE-6-PHOSPHATE ISOMERASE

Template:ABSTRACT PUBMED 11752775

About this Structure

1FS5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase., Rudino-Pinera E, Morales-Arrieta S, Rojas-Trejo SP, Horjales E, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):10-20. Epub 2001, Dec 21. PMID:11752775

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