1im8

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(New page: 200px<br /><applet load="1im8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1im8, resolution 2.2&Aring;" /> '''Crystal structure of ...)
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[[Image:1im8.gif|left|200px]]<br /><applet load="1im8" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Crystal structure of YecO from Haemophilus influenzae (HI0319), a methyltransferase with a bound S-adenosylhomocysteine'''<br />
'''Crystal structure of YecO from Haemophilus influenzae (HI0319), a methyltransferase with a bound S-adenosylhomocysteine'''<br />
==Overview==
==Overview==
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The crystal structure of YecO from Haemophilus influenzae (HI0319), a, protein annotated in the sequence databases as hypothetical, and that has, not been assigned a function, has been determined at 2.2-A resolution. The, structure reveals a fold typical of S-adenosyl-L-methionine-dependent, (AdoMet) methyltransferase enzymes. Moreover, a processed cofactor, S-adenosyl-L-homocysteine (AdoHcy), is bound to the enzyme, further, confirming the biochemical function of HI0319 and its sequence family, members. An active site arginine, shielded from bulk solvent, interacts, with an anion, possibly a chloride ion, which in turn interacts with the, sulfur atom of AdoHcy. The AdoHcy and nearby protein residues delineate a, small solvent-excluded substrate binding cavity of 162 A(3) in volume. The, environment surrounding the cavity indicates that the substrate molecule, contains a hydrophobic moiety and an anionic group. Many of the residues, that define the cavity are invariant in the HI0319 sequence family but are, not conserved in other methyltransferases. Therefore, the substrate, specificity of YecO enzymes is unique and differs from the substrate, specificity of all other methyltransferases sequenced to date. Examination, of the Enzyme Commission list of methyltransferases prompted a manual, inspection of 10 possible substrates using computer graphics and suggested, that the ortho-substituted benzoic acids fit best in the active site.
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The crystal structure of YecO from Haemophilus influenzae (HI0319), a protein annotated in the sequence databases as hypothetical, and that has not been assigned a function, has been determined at 2.2-A resolution. The structure reveals a fold typical of S-adenosyl-L-methionine-dependent (AdoMet) methyltransferase enzymes. Moreover, a processed cofactor, S-adenosyl-L-homocysteine (AdoHcy), is bound to the enzyme, further confirming the biochemical function of HI0319 and its sequence family members. An active site arginine, shielded from bulk solvent, interacts with an anion, possibly a chloride ion, which in turn interacts with the sulfur atom of AdoHcy. The AdoHcy and nearby protein residues delineate a small solvent-excluded substrate binding cavity of 162 A(3) in volume. The environment surrounding the cavity indicates that the substrate molecule contains a hydrophobic moiety and an anionic group. Many of the residues that define the cavity are invariant in the HI0319 sequence family but are not conserved in other methyltransferases. Therefore, the substrate specificity of YecO enzymes is unique and differs from the substrate specificity of all other methyltransferases sequenced to date. Examination of the Enzyme Commission list of methyltransferases prompted a manual inspection of 10 possible substrates using computer graphics and suggested that the ortho-substituted benzoic acids fit best in the active site.
==About this Structure==
==About this Structure==
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1IM8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with CL and SAI as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IM8 OCA].
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1IM8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=SAI:'>SAI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IM8 OCA].
==Reference==
==Reference==
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[[Category: Howard, A.]]
[[Category: Howard, A.]]
[[Category: Lim, K.]]
[[Category: Lim, K.]]
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[[Category: S2F, Structure.2.Function.Project.]]
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[[Category: S2F, Structure 2.Function Project.]]
[[Category: Tempczyk, A.]]
[[Category: Tempczyk, A.]]
[[Category: Toedt, J.]]
[[Category: Toedt, J.]]
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[[Category: structure 2 function project]]
[[Category: structure 2 function project]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:30:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:17 2008''

Revision as of 11:13, 21 February 2008

Image:1im8.gif

1im8, resolution 2.2Å

Drag the structure with the mouse to rotate

Crystal structure of YecO from Haemophilus influenzae (HI0319), a methyltransferase with a bound S-adenosylhomocysteine

Overview

The crystal structure of YecO from Haemophilus influenzae (HI0319), a protein annotated in the sequence databases as hypothetical, and that has not been assigned a function, has been determined at 2.2-A resolution. The structure reveals a fold typical of S-adenosyl-L-methionine-dependent (AdoMet) methyltransferase enzymes. Moreover, a processed cofactor, S-adenosyl-L-homocysteine (AdoHcy), is bound to the enzyme, further confirming the biochemical function of HI0319 and its sequence family members. An active site arginine, shielded from bulk solvent, interacts with an anion, possibly a chloride ion, which in turn interacts with the sulfur atom of AdoHcy. The AdoHcy and nearby protein residues delineate a small solvent-excluded substrate binding cavity of 162 A(3) in volume. The environment surrounding the cavity indicates that the substrate molecule contains a hydrophobic moiety and an anionic group. Many of the residues that define the cavity are invariant in the HI0319 sequence family but are not conserved in other methyltransferases. Therefore, the substrate specificity of YecO enzymes is unique and differs from the substrate specificity of all other methyltransferases sequenced to date. Examination of the Enzyme Commission list of methyltransferases prompted a manual inspection of 10 possible substrates using computer graphics and suggested that the ortho-substituted benzoic acids fit best in the active site.

About this Structure

1IM8 is a Single protein structure of sequence from Haemophilus influenzae with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of YecO from Haemophilus influenzae (HI0319) reveals a methyltransferase fold and a bound S-adenosylhomocysteine., Lim K, Zhang H, Tempczyk A, Bonander N, Toedt J, Howard A, Eisenstein E, Herzberg O, Proteins. 2001 Dec 1;45(4):397-407. PMID:11746687

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