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1vkr

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{{STRUCTURE_1vkr| PDB=1vkr | SCENE= }}
{{STRUCTURE_1vkr| PDB=1vkr | SCENE= }}
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'''STRUCTURE OF IIB DOMAIN OF THE MANNITOL-SPECIFIC PERMEASE ENZYME II'''
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===STRUCTURE OF IIB DOMAIN OF THE MANNITOL-SPECIFIC PERMEASE ENZYME II===
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==Overview==
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The solution structure of the cytoplasmic B domain of the mannitol (Mtl) transporter (II(Mtl)) from the mannitol branch of the Escherichia coli phosphotransferase system has been solved by multidimensional NMR spectroscopy with extensive use of residual dipolar couplings. The ordered IIB(Mtl) domain (residues 375-471 of II(Mtl)) consists of a four-stranded parallel beta-sheet flanked by two helices (alpha(1) and alpha(3)) on one face and helix alpha(2) on the opposite face with a characteristic Rossmann fold comprising two right-handed beta(1)alpha(1)beta(2) and beta(3)alpha(2)beta(4) motifs. The active site loop is structurally very similar to that of the eukaryotic protein tyrosine phosphatases, with the active site cysteine (Cys-384) primed in the thiolate state (pK(a) &lt; 5.6) for nucleophilic attack at the phosphorylated histidine (His-554) of the IIA(Mtl) domain through stabilization by hydrogen bonding interactions with neighboring backbone amide groups at positions i + 2/3/4 from Cys-384 and with the hydroxyl group of Ser-391 at position i + 7. Modeling of the phosphorylated state of IIB(Mtl) suggests that the phosphoryl group can be readily stabilized by hydrogen bonding interactions with backbone amides in the i + 2/4/5/6/7 positions as well as with the hydroxyl group of Ser390 at position i + 6. Despite the absence of any significant sequence identity, the structure of IIB(Mtl) is remarkably similar to the structures of bovine protein tyrosine phosphatase (which contains two long insertions relative to IIB(Mtl)) and the cytoplasmic B component of enzyme II(Chb), which fulfills an analogous role to IIB(Mtl) in the N,N'-diacetylchitobiose branch of the phosphotransferase system. All three proteins utilize a cysteine residue in the nucleophilic attack of a phosphoryl group covalently bound to another protein.
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{{ABSTRACT_PUBMED_15258141}}
==About this Structure==
==About this Structure==
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1VKR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VKR OCA].
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1VKR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VKR OCA].
==Reference==
==Reference==
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[[Category: Sugar transport]]
[[Category: Sugar transport]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:39:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:59:42 2008''

Revision as of 16:59, 28 July 2008

Image:1vkr.png

Template:STRUCTURE 1vkr

STRUCTURE OF IIB DOMAIN OF THE MANNITOL-SPECIFIC PERMEASE ENZYME II

Template:ABSTRACT PUBMED 15258141

About this Structure

1VKR is a Single protein structure of sequence from Escherichia coli o157:h7. Full experimental information is available from OCA.

Reference

Three-dimensional solution structure of the cytoplasmic B domain of the mannitol transporter IImannitol of the Escherichia coli phosphotransferase system., Legler PM, Cai M, Peterkofsky A, Clore GM, J Biol Chem. 2004 Sep 10;279(37):39115-21. Epub 2004 Jul 15. PMID:15258141

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