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.


1qzz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qzz.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1qzz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qzz| PDB=1qzz | SCENE= }}
{{STRUCTURE_1qzz| PDB=1qzz | SCENE= }}
-
'''Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-methionine (SAM)'''
+
===Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-methionine (SAM)===
-
==Overview==
+
<!--
-
Anthracyclines are aromatic polyketide antibiotics, and several of these compounds are widely used as anti-tumor drugs in chemotherapy. Aclacinomycin-10-hydroxylase (RdmB) is one of the tailoring enzymes that modify the polyketide backbone in the biosynthesis of these metabolites. RdmB, a S-adenosyl-L-methionine-dependent methyltransferase homolog, catalyses the hydroxylation of 15-demethoxy-epsilon-rhodomycin to beta-rhodomycin, one step in rhodomycin biosynthesis in Streptomyces purpurascens. The crystal structure of RdmB, determined by multiwavelength anomalous diffraction to 2.1A resolution, reveals that the enzyme subunit has a fold similar to methyltransferases and binds S-adenosyl-L-methionine. The N-terminal domain, which consists almost exclusively of alpha-helices, is involved in dimerization. The C-terminal domain contains a typical alpha/beta nucleotide-binding fold, which binds S-adenosyl-L-methionine, and several of the residues interacting with the cofactor are conserved in O-methyltransferases. Adjacent to the S-adenosyl-L-methionine molecule there is a large cleft extending to the enzyme surface of sufficient size to bind the substrate. Analysis of the putative substrate-binding pocket suggests that there is no enzymatic group in proximity of the substrate 15-demethoxy-epsilon-rhodomycin, which could assist in proton abstraction and thus facilitate methyl transfer. The lack of a suitably positioned catalytic base might thus be one of the features responsible for the inability of the enzyme to act as a methyltransferase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14607118}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14607118 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14607118}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
[[Category: Tailoring enzyme]]
[[Category: Tailoring enzyme]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:10:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:10:16 2008''

Revision as of 01:10, 28 July 2008

Image:1qzz.png

Template:STRUCTURE 1qzz

Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adensyl-L-methionine (SAM)

Template:ABSTRACT PUBMED 14607118

About this Structure

1QZZ is a Single protein structure of sequence from Streptomyces purpurascens. Full crystallographic information is available from OCA.

Reference

Crystal structure of aclacinomycin-10-hydroxylase, a S-adenosyl-L-methionine-dependent methyltransferase homolog involved in anthracycline biosynthesis in Streptomyces purpurascens., Jansson A, Niemi J, Lindqvist Y, Mantsala P, Schneider G, J Mol Biol. 2003 Nov 21;334(2):269-80. PMID:14607118

Page seeded by OCA on Mon Jul 28 04:10:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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