We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2pt6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pt6.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2pt6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pt6| PDB=2pt6 | SCENE= }}
{{STRUCTURE_2pt6| PDB=2pt6 | SCENE= }}
-
'''The structure of Plasmodium falciparum spermidine synthase in complex with decarboxylated S-adenosylmethionine'''
+
===The structure of Plasmodium falciparum spermidine synthase in complex with decarboxylated S-adenosylmethionine===
-
==Overview==
+
<!--
-
Plasmodium falciparum is the causative agent of the most severe type of malaria, a life-threatening disease affecting the lives of over three billion people. Factors like widespread resistance against available drugs and absence of an effective vaccine are seriously compounding control of the malaria parasite. Thus, there is an urgent need for the identification and validation of new drug targets. The enzymes of the polyamine biosynthesis pathway have been suggested as possible targets for the treatment of malaria. One of these enzymes is spermidine synthase (SPDS, putrescine aminopropyltransferase), which catalyzes the transfer of an aminopropyl moiety from decarboxylated S-adenosylmethionine (dcAdoMet) to putrescine, leading to the formation of spermidine and 5'-methylthioadenosine. Here we present the three-dimensional structure of P. falciparum spermidine synthase (pfSPDS) in apo form, in complex with dcAdoMet and two inhibitors, S-adenosyl-1,8-diamino-3-thio-octane (AdoDATO) and trans-4-methylcyclohexylamine (4MCHA). The results show that binding of dcAdoMet to pfSPDS stabilizes the conformation of the flexible gatekeeper loop of the enzyme and affects the conformation of the active-site amino acid residues, preparing the protein for binding of the second substrate. The complexes of AdoDATO and 4MCHA with pfSPDS reveal the mode of interactions of these compounds with the enzyme. While AdoDATO essentially fills the entire active-site pocket, 4MCHA only occupies part of it, which suggests that simple modifications of this compound may yield more potent inhibitors of pfSPDS.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17822713}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17822713 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17822713}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Structural genomics consortium]]
[[Category: Structural genomics consortium]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:45:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:01:04 2008''

Revision as of 16:01, 27 July 2008

Image:2pt6.png

Template:STRUCTURE 2pt6

The structure of Plasmodium falciparum spermidine synthase in complex with decarboxylated S-adenosylmethionine

Template:ABSTRACT PUBMED 17822713

About this Structure

2PT6 is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.

Reference

Crystal structure of Plasmodium falciparum spermidine synthase in complex with the substrate decarboxylated S-adenosylmethionine and the potent inhibitors 4MCHA and AdoDATO., Dufe VT, Qiu W, Muller IB, Hui R, Walter RD, Al-Karadaghi S, J Mol Biol. 2007 Oct 12;373(1):167-77. Epub 2007 Aug 2. PMID:17822713

Page seeded by OCA on Sun Jul 27 19:01:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pt6"
Personal tools