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2dt9

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Revision as of 14:44, 11 September 2015

Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus

Structural highlights

2dt9 is a 2 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2dtj
Gene:	askB ("Flavobacterium thermophilum" Yoshida and Oshima 1971)
Activity:	Aspartate kinase, with EC number 2.7.2.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[AK_THETH] Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase (AK; EC 2.7.2.4) from Thermus thermophilus (TtAKbeta) were determined at 2.15 A in the Thr-bound form (TtAKbeta-Thr) and at 2.98 A in the Thr-free form (TtAKbeta-free). Although both forms are crystallized as dimers, the contact surface area of the dimer interface in TtAKbeta-free (3200 A(2)) is smaller than that of TtAKbeta-Thr (3890 A(2)). Sedimentation equilibrium analyzed by ultracentrifugation revealed that TtAKbeta is present in equilibrium between a monomer and dimer, and that Thr binding shifts the equilibrium to dimer formation. In the absence of Thr, an outward shift of beta-strands near the Thr-binding site (site 1) and a concomitant loss of the electron density of the loop region between beta3 and beta4 near the Thr-binding site are observed. The mechanism of regulation by Thr is discussed on the basis of the crystal structures. TtAKbeta has higher thermostability than the regulatory subunit of Corynebacterium glutamicum AK, with a difference in denaturation temperature (T(m)) of 40 degrees C. Comparison of the crystal structures of TtAKbeta and the regulatory subunit of C. glutamicum AK showed that the well-packed hydrophobic core and high Pro content in loops contribute to the high thermostability of TtAKbeta.

Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase from Thermus thermophilus.,Yoshida A, Tomita T, Kono H, Fushinobu S, Kuzuyama T, Nishiyama M FEBS J. 2009 Jun;276(11):3124-36. Epub 2009 Apr 23. PMID:19490113^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nishiyama M, Kukimoto M, Beppu T, Horinouchi S. An operon encoding aspartokinase and purine phosphoribosyltransferase in Thermus flavus. Microbiology. 1995 May;141 ( Pt 5):1211-9. PMID:7773416
↑ Kobashi N, Nishiyama M, Tanokura M. Kinetic and mutation analyses of aspartate kinase from Thermus flavus. J Biosci Bioeng. 1999;87(6):739-45. PMID:16232547
↑ Yoshida A, Tomita T, Kono H, Fushinobu S, Kuzuyama T, Nishiyama M. Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase from Thermus thermophilus. FEBS J. 2009 Jun;276(11):3124-36. Epub 2009 Apr 23. PMID:19490113 doi:10.1111/j.1742-4658.2009.07030.x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2dt9"

@@ Line 2: / Line 2: @@
 <StructureSection load='2dt9' size='340' side='right' caption='[[2dt9]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2dt9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DT9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DT9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2dt9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DT9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DT9 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dtj|2dtj]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">askB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">askB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dt9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dt9 RCSB], [http://www.ebi.ac.uk/pdbsum/2dt9 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dt9 OCA], [http://pdbe.org/2dt9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dt9 RCSB], [http://www.ebi.ac.uk/pdbsum/2dt9 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2dt9" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
 [[Category: Aspartate kinase]]
-[[Category: Thermus thermophilus]]
 [[Category: Fushinobu, S]]
 [[Category: Kuzuyama, T]]

2dt9

From Proteopedia

Revision as of 14:44, 11 September 2015

Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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