2aaz

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[[Image:2aaz.gif|left|200px]]<br /><applet load="2aaz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2aaz.gif|left|200px]]
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caption="2aaz, resolution 2.08&Aring;" />
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'''Cryptococcus neoformans thymidylate synthase complexed with substrate and an antifolate'''<br />
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{{Structure
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|PDB= 2aaz |SIZE=350|CAPTION= <scene name='initialview01'>2aaz</scene>, resolution 2.08&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=UMP:2'-DEOXYURIDINE+5'-MONOPHOSPHATE'>UMP</scene> and <scene name='pdbligand=CB3:10-PROPARGYL-5,8-DIDEAZAFOLIC ACID'>CB3</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45]
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|GENE= TMP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5207 Filobasidiella neoformans])
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}}
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'''Cryptococcus neoformans thymidylate synthase complexed with substrate and an antifolate'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2AAZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Filobasidiella_neoformans Filobasidiella neoformans] with <scene name='pdbligand=UMP:'>UMP</scene> and <scene name='pdbligand=CB3:'>CB3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAZ OCA].
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2AAZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Filobasidiella_neoformans Filobasidiella neoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAZ OCA].
==Reference==
==Reference==
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The structure of Cryptococcus neoformans thymidylate synthase suggests strategies for using target dynamics for species-specific inhibition., Finer-Moore JS, Anderson AC, O'Neil RH, Costi MP, Ferrari S, Krucinski J, Stroud RM, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1320-34. Epub 2005, Sep 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16204883 16204883]
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The structure of Cryptococcus neoformans thymidylate synthase suggests strategies for using target dynamics for species-specific inhibition., Finer-Moore JS, Anderson AC, O'Neil RH, Costi MP, Ferrari S, Krucinski J, Stroud RM, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1320-34. Epub 2005, Sep 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16204883 16204883]
[[Category: Filobasidiella neoformans]]
[[Category: Filobasidiella neoformans]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:47:32 2008''

Revision as of 13:47, 20 March 2008


PDB ID 2aaz

Drag the structure with the mouse to rotate
, resolution 2.08Å
Ligands: and
Gene: TMP1 (Filobasidiella neoformans)
Activity: Thymidylate synthase, with EC number 2.1.1.45
Coordinates: save as pdb, mmCIF, xml



Cryptococcus neoformans thymidylate synthase complexed with substrate and an antifolate


Overview

The ternary complex crystal structures of Cryptococcus neoformans and Escherichia coli thymidylate synthase (TS) suggest mechanisms of species-specific inhibition of a highly conserved protein. The 2.1 Angstrom structure of C. neoformans TS cocrystallized with substrate and the cofactor analog CB3717 shows that the binding sites for substrate and cofactor are highly conserved with respect to human TS, but that the structure of the cofactor-binding site of C. neoformans TS is less constrained by surrounding residues. This feature might allow C. neoformans TS to form TS-dUMP-inhibitor complexes with a greater range of antifolates than human TS. 3',3-Dibromophenol-4-chloro-1,8-naphthalein (GA9) selectively inhibits both E. coli TS and C. neoformans TS (K(i) = 4 microM) over human TS (K(i) >> 245 microM). The E. coli TS-dUMP-GA9 complex is in an open conformation, similar to that of the apoenzyme crystal structure. The GA9-binding site overlaps the binding site of the pABA-glutamyl moiety of the cofactor. The fact that human apoTS can adopt an unusual fold in which the GA9-binding site is disordered may explain the poor affinity of GA9 for the human enzyme. These observations highlight the critical need to incorporate multiple target conformations in any computational attempt to facilitate drug discovery.

About this Structure

2AAZ is a Single protein structure of sequence from Filobasidiella neoformans. Full crystallographic information is available from OCA.

Reference

The structure of Cryptococcus neoformans thymidylate synthase suggests strategies for using target dynamics for species-specific inhibition., Finer-Moore JS, Anderson AC, O'Neil RH, Costi MP, Ferrari S, Krucinski J, Stroud RM, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1320-34. Epub 2005, Sep 28. PMID:16204883

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