1bkp

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[[Image:1bkp.gif|left|200px]]<br /><applet load="1bkp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bkp.gif|left|200px]]
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caption="1bkp, resolution 1.70&Aring;" />
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'''THERMOSTABLE THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS'''<br />
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{{Structure
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|PDB= 1bkp |SIZE=350|CAPTION= <scene name='initialview01'>1bkp</scene>, resolution 1.70&Aring;
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|SITE= <scene name='pdbsite=CAA:Catalytic+CYS'>CAA</scene> and <scene name='pdbsite=CAB:Catalytic+CYS'>CAB</scene>
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|LIGAND=
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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= THYA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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}}
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'''THERMOSTABLE THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1BKP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. 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] Known structural/functional Sites: <scene name='pdbsite=CAA:Catalytic+CYS'>CAA</scene> and <scene name='pdbsite=CAB:Catalytic+CYS'>CAB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKP OCA].
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1BKP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BKP OCA].
==Reference==
==Reference==
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Crystal structures of a unique thermal-stable thymidylate synthase from Bacillus subtilis., Stout TJ, Schellenberger U, Santi DV, Stroud RM, Biochemistry. 1998 Oct 20;37(42):14736-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9778348 9778348]
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Crystal structures of a unique thermal-stable thymidylate synthase from Bacillus subtilis., Stout TJ, Schellenberger U, Santi DV, Stroud RM, Biochemistry. 1998 Oct 20;37(42):14736-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9778348 9778348]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: methyltransferase]]
[[Category: methyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:12:24 2008''

Revision as of 08:12, 20 March 2008


PDB ID 1bkp

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites: and
Gene: THYA (Bacillus subtilis)
Activity: Thymidylate synthase, with EC number 2.1.1.45
Coordinates: save as pdb, mmCIF, xml



THERMOSTABLE THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS


Overview

Unlike all other organisms studied to date, Bacillus subtilis expresses two different thymidylate synthases: bsTS-A and bsTS-B. bsTS-A displays enhanced enzymatic and structural thermal stability uncharacteristic of most TSs. Despite the high level of TS conservation across most species, bsTS-A shares low sequence identity (<40%) with the majority of TSs from other organisms. This TS and the TSs from Lactococcus lactis and phage Phi3T-to which it is most similar-have been of interest for some time since, by structure-based sequence alignment, they appear to lack several key residues shown by mutagenesis to be essential to enzymatic function [Greene, P. J., Yu, P. L., Zhao, J., Schiffer, C. A., and Santi, D. (1994) Protein Sci. 3, 1114-6]. In addition, bsTS-A demonstrates specific activity 2-3-fold higher than TS from Lactobacillus casei or Escherichia coli. We have solved the crystal structure of this unusual TS in four crystal forms to a maximum resolution of 1.7 A. Each of these crystal forms contains either one or two noncrystallographically related dimers. Stabilization of the beta-sheet dimer interface through a dramatic architecture of buttressed internal salt bridges maintains the structural integrity of bsTS-A at elevated temperatures. Melting curves of TSs from L. casei and E. coli are compared to that of TS-A from B. subtilis and correlated with numbers of hydrogen bonds, salt bridges, and the numbers of interactions localized to the dimer interface. Analysis of this structure will shed light on the conservation of function across diversity of sequence, as well as provide insights into the thermal stabilization of a highly conserved enzyme.

About this Structure

1BKP is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Crystal structures of a unique thermal-stable thymidylate synthase from Bacillus subtilis., Stout TJ, Schellenberger U, Santi DV, Stroud RM, Biochemistry. 1998 Oct 20;37(42):14736-47. PMID:9778348

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