1jbw

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[[Image:1jbw.gif|left|200px]]<br /><applet load="1jbw" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jbw.gif|left|200px]]
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caption="1jbw, resolution 1.85&Aring;" />
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'''FPGS-AMPPCP-folate complex'''<br />
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{{Structure
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|PDB= 1jbw |SIZE=350|CAPTION= <scene name='initialview01'>1jbw</scene>, resolution 1.85&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ACQ:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACQ</scene> and <scene name='pdbligand=TMF:5,10-METHYLENE-6-HYDROFOLIC ACID'>TMF</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Tetrahydrofolate_synthase Tetrahydrofolate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.17 6.3.2.17]
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|GENE=
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}}
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'''FPGS-AMPPCP-folate complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1JBW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ACQ:'>ACQ</scene> and <scene name='pdbligand=TMF:'>TMF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Tetrahydrofolate_synthase Tetrahydrofolate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.17 6.3.2.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBW OCA].
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1JBW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBW OCA].
==Reference==
==Reference==
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Folate-binding triggers the activation of folylpolyglutamate synthetase., Sun X, Cross JA, Bognar AL, Baker EN, Smith CA, J Mol Biol. 2001 Jul 27;310(5):1067-78. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11501996 11501996]
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Folate-binding triggers the activation of folylpolyglutamate synthetase., Sun X, Cross JA, Bognar AL, Baker EN, Smith CA, J Mol Biol. 2001 Jul 27;310(5):1067-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11501996 11501996]
[[Category: Lactobacillus casei]]
[[Category: Lactobacillus casei]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: fpgs folate amppcp ternary complex]]
[[Category: fpgs folate amppcp ternary complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:01:18 2008''

Revision as of 10:01, 20 March 2008


PDB ID 1jbw

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands: , and
Activity: Tetrahydrofolate synthase, with EC number 6.3.2.17
Coordinates: save as pdb, mmCIF, xml



FPGS-AMPPCP-folate complex


Overview

Folic acid is an essential vitamin for normal cell growth, primarily through its central role in one-carbon metabolism. Folate analogs (antifolates) are targeted at the same reactions and are widely used as therapeutic drugs for cancer and bacterial infections. Effective retention of folates in cells and the efficacy of antifolate drugs both depend upon the addition of a polyglutamate tail to the folate or antifolate molecule by the enzyme folylpolyglutamate synthetase (FPGS). The reaction mechanism involves the ATP-dependent activation of the free carboxylate group on the folate molecule to give an acyl phosphate intermediate, followed by attack by the incoming L-glutamate substrate. FPGS shares a number of structural and mechanistic details with the bacterial cell wall ligases MurD, MurE and MurF, and these enzymes, along with FPGS, form a subfamily of the ADP-forming amide bond ligase family. High-resolution crystallographic analyses of binary and ternary complexes of Lactobacillus casei FPGS reveal that binding of the first substrate (ATP) is not sufficient to generate an active enzyme. However, binding of folate as the second substrate triggers a large conformational change that activates FPGS and allows the enzyme to adopt a form that is then able to bind the third substrate, L-glutamate, and effect the addition of a polyglutamate tail to the folate.

About this Structure

1JBW is a Single protein structure of sequence from Lactobacillus casei. Full crystallographic information is available from OCA.

Reference

Folate-binding triggers the activation of folylpolyglutamate synthetase., Sun X, Cross JA, Bognar AL, Baker EN, Smith CA, J Mol Biol. 2001 Jul 27;310(5):1067-78. PMID:11501996

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