1s3i

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[[Image:1s3i.jpg|left|200px]]<br /><applet load="1s3i" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1s3i.jpg|left|200px]]
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caption="1s3i, resolution 2.30&Aring;" />
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'''Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase'''<br />
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{{Structure
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|PDB= 1s3i |SIZE=350|CAPTION= <scene name='initialview01'>1s3i</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6]
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|GENE= FTHFD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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}}
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'''Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1S3I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3I OCA].
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1S3I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S3I OCA].
==Reference==
==Reference==
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The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain., Chumanevich AA, Krupenko SA, Davies C, J Biol Chem. 2004 Apr 2;279(14):14355-64. Epub 2004 Jan 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14729668 14729668]
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The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain., Chumanevich AA, Krupenko SA, Davies C, J Biol Chem. 2004 Apr 2;279(14):14355-64. Epub 2004 Jan 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14729668 14729668]
[[Category: Formyltetrahydrofolate dehydrogenase]]
[[Category: Formyltetrahydrofolate dehydrogenase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: rossmann fold]]
[[Category: rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:59:55 2008''

Revision as of 11:59, 20 March 2008


PDB ID 1s3i

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands:
Gene: FTHFD (Rattus norvegicus)
Activity: Formyltetrahydrofolate dehydrogenase, with EC number 1.5.1.6
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase


Overview

10-Formyltetrahydrofolate dehydrogenase (FDH) converts 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: a hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and a NADP(+)-dependent dehydrogenase domain that reduces the formyl to carbon dioxide. As a first step toward deciphering the catalytic mechanism of the enzyme, we have determined the crystal structure of the hydrolase domain of FDH from rat, solved to 2.3-A resolution. The structure comprises two domains. As expected, domain 1 shares the same Rossmann fold as the related enzymes, methionyl-tRNA-formyltransferase and glycinamide ribonucleotide formyltransferase, but, unexpectedly, the structural similarity between the amino-terminal domain of 10-formyltetrahydrofolate dehydrogenase and methionyl-tRNA-formyltransferase extends to the C terminus of both proteins. The active site contains a molecule of beta-mercaptoethanol that is positioned between His-106 and Asp-142 and that appears to mimic the formate product. We propose a catalytic mechanism for the hydrolase reaction in which Asp-142 polarizes the catalytic water molecule and His-106 orients the carbonyl group of formyl. The structure also provides clues as to how, in the native enzyme, the hydrolase domain transfers its product to the dehydrogenase domain.

About this Structure

1S3I is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain., Chumanevich AA, Krupenko SA, Davies C, J Biol Chem. 2004 Apr 2;279(14):14355-64. Epub 2004 Jan 16. PMID:14729668

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