This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1im8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1im8.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1im8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1im8| PDB=1im8 | SCENE= }}
{{STRUCTURE_1im8| PDB=1im8 | SCENE= }}
-
'''Crystal structure of YecO from Haemophilus influenzae (HI0319), a methyltransferase with a bound S-adenosylhomocysteine'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11746687}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11746687 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11746687}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structure 2 function project]]
[[Category: Structure 2 function project]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:09:12 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:31:40 2008''

Revision as of 10:31, 1 July 2008

Image:1im8.png

Template:STRUCTURE 1im8

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

Template:ABSTRACT PUBMED 11746687

About this Structure

1IM8 is a Single protein structure of sequence from Haemophilus influenzae. 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

Page seeded by OCA on Tue Jul 1 13:31:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1im8"
Personal tools