From Proteopedia
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| - | [[Image:1hka.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1hka| PDB=1hka | SCENE= }} | | {{STRUCTURE_1hka| PDB=1hka | SCENE= }} |
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| - | '''6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE'''
| + | ===6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE=== |
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| - | ==Overview==
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| - | BACKGROUND: Folate cofactors are essential for life. Mammals derive folates from their diet, whereas most microorganisms must synthesize folates de novo. Enzymes of the folate pathway therefore provide ideal targets for the development of antimicrobial agents. 6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the transfer of pyrophosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP), the first reaction in the folate biosynthetic pathway. RESULTS: The crystal structure of HPPK from Escherichia coli has been determined at 1.5 A resolution with a crystallographic R factor of 0.182. The HPPK molecule has a novel three-layered alpha beta alpha fold that creates a valley approximately 26 A long, 10 A wide and 10 A deep. The active center of HPPK is located in the valley and the substrate-binding sites have been identified with the aid of NMR spectroscopy. The HP-binding site is located at one end of the valley, near Asn55, and is sandwiched between two aromatic sidechains. The ATP-binding site is located at the other end of the valley. The adenine base of ATP is positioned near Leu111 and the ribose and the triphosphate extend across and reach the vicinity of HP. CONCLUSIONS: The HPPK structure provides a framework to elucidate structure/function relationships of the enzyme and to analyze mechanisms of pyrophosphoryl transfer. Furthermore, this work may prove useful in the structure-based design of new antimicrobial agents.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10378268}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10378268 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10378268}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pyrophosphokinase]] | | [[Category: Pyrophosphokinase]] |
| | [[Category: Pyrophosphoryl transfer]] | | [[Category: Pyrophosphoryl transfer]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:56:17 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:18:22 2008'' |
Revision as of 05:18, 1 July 2008
Template:STRUCTURE 1hka
6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE
Template:ABSTRACT PUBMED 10378268
About this Structure
1HKA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents., Xiao B, Shi G, Chen X, Yan H, Ji X, Structure. 1999 May;7(5):489-96. PMID:10378268
Page seeded by OCA on Tue Jul 1 08:18:22 2008
