2veg: Difference between revisions

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[[Image:2veg.jpg|left|200px]]
{{Seed}}
[[Image:2veg.png|left|200px]]


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{{STRUCTURE_2veg|  PDB=2veg  |  SCENE=  }}  
{{STRUCTURE_2veg|  PDB=2veg  |  SCENE=  }}  


'''DIHYDROPTEROATE SYNTHASE FROM STREPTOCOCCUS PNEUMONIAE: COMPLEX WITH 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN MONOPHOSPHATE'''
===DIHYDROPTEROATE SYNTHASE FROM STREPTOCOCCUS PNEUMONIAE: COMPLEX WITH 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN MONOPHOSPHATE===




==Overview==
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Dihydropteroate synthase (DHPS) catalyses an essential step in the biosynthesis of folic acid and is the target for the sulfonamide group of antimicrobial drugs. Here we report two crystal structures of DHPS from the respiratory pathogen Streptococcus pneumoniae: the apoenzyme at 1.8-A resolution and a complex with 6-hydroxymethyl-7,8-dihydropterin monophosphate at 2.4-A resolution. The enzyme forms a alpha/beta barrel structure, with a highly conserved binding pocket for recognition of the pterin substrate, 6-hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPPP). There is a fixed order of substrate binding: DHPPP binds first, followed by the second substrate, para-aminobenzoic acid (pABA). Binding of pyrophosphate also allows the enzyme to recognise pABA or sulfonamide drugs, which act as pABA analogues. Using equilibrium and pre-steady state kinetic fluorescence measurements, we show that the on-rate for DHPPP binding to the enzyme is relatively slow (2.6 x 105 M-1s-1) and propose that binding of this substrate induces a large scale movement of the second loop in the enzyme structure, to participate in formation of the pABA binding site. Two mutations, which confer resistance to sulfonamide drugs, do not affect DHPPP binding but have a substantial effect on pABA and sulfonamide recognition. The results show that binding of DHPPP and pABA are separate, distinguishable events in the reaction cycle, and that mutations which confer resistance to sulfonamide drugs act exclusively on the second step in the binding process.
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{{ABSTRACT_PUBMED_18321242}}


==About this Structure==
==About this Structure==
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[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
[[Category: Transferase]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:39:42 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:13:41 2008''

Revision as of 02:13, 28 July 2008

File:2veg.png

Template:STRUCTURE 2veg

DIHYDROPTEROATE SYNTHASE FROM STREPTOCOCCUS PNEUMONIAE: COMPLEX WITH 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN MONOPHOSPHATE

Template:ABSTRACT PUBMED 18321242

About this Structure

2VEG is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

Reference

Dihydropteroate synthase from Streptococcus pneumoniae: structure, ligand recognition and mechanism of sulfonamide resistance., Levy C, Minnis D, Derrick JP, Biochem J. 2008 Mar 5;. PMID:18321242

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