1uc8: Difference between revisions

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Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8

OverviewOverview

The thermophilic bacterium Thermus thermophilus synthesizes lysine through the alpha-aminoadipate pathway, which uses alpha-aminoadipate as a biosynthetic intermediate of lysine. LysX is the essential enzyme in this pathway, and is believed to catalyze the acylation of alpha-aminoadipate. We have determined the crystal structures of LysX and its complex with ADP at 2.0A and 2.38A resolutions, respectively. LysX is composed of three alpha+beta domains, each composed of a four to five-stranded beta-sheet core flanked by alpha-helices. The C-terminal and central domains form an ATP-grasp fold, which is responsible for ATP binding. LysX has two flexible loop regions, which are expected to play an important role in substrate binding and protection. In spite of the low level of sequence identity, the overall fold of LysX is surprisingly similar to that of other ATP-grasp fold proteins, such as D-Ala:D-Ala ligase, PurT-encoded glycinamide ribonucleotide transformylase, glutathione synthetase, and synapsin I. In particular, they share a similar spatial arrangement of the amino acid residues around the ATP-binding site. This observation strongly suggests that LysX is an ATP-utilizing enzyme that shares a common evolutionary ancestor with other ATP-grasp fold proteins possessing a carboxylate-amine/thiol ligase activity.

About this StructureAbout this Structure

1UC8 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a lysine biosynthesis enzyme, LysX, from Thermus thermophilus HB8., Sakai H, Vassylyeva MN, Matsuura T, Sekine S, Gotoh K, Nishiyama M, Terada T, Shirouzu M, Kuramitsu S, Vassylyev DG, Yokoyama S, J Mol Biol. 2003 Sep 19;332(3):729-40. PMID:12963379

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 caption="1uc8, resolution 2.0&Aring;" />
 '''Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8'''<br />
 ==Overview==
-The thermophilic bacterium Thermus thermophilus synthesizes lysine through, the alpha-aminoadipate pathway, which uses alpha-aminoadipate as a, biosynthetic intermediate of lysine. LysX is the essential enzyme in this, pathway, and is believed to catalyze the acylation of alpha-aminoadipate., We have determined the crystal structures of LysX and its complex with ADP, at 2.0A and 2.38A resolutions, respectively. LysX is composed of three, alpha+beta domains, each composed of a four to five-stranded beta-sheet, core flanked by alpha-helices. The C-terminal and central domains form an, ATP-grasp fold, which is responsible for ATP binding. LysX has two, flexible loop regions, which are expected to play an important role in, substrate binding and protection. In spite of the low level of sequence, identity, the overall fold of LysX is surprisingly similar to that of, other ATP-grasp fold proteins, such as D-Ala:D-Ala ligase, PurT-encoded, glycinamide ribonucleotide transformylase, glutathione synthetase, and, synapsin I. In particular, they share a similar spatial arrangement of the, amino acid residues around the ATP-binding site. This observation strongly, suggests that LysX is an ATP-utilizing enzyme that shares a common, evolutionary ancestor with other ATP-grasp fold proteins possessing a, carboxylate-amine/thiol ligase activity.
+The thermophilic bacterium Thermus thermophilus synthesizes lysine through the alpha-aminoadipate pathway, which uses alpha-aminoadipate as a biosynthetic intermediate of lysine. LysX is the essential enzyme in this pathway, and is believed to catalyze the acylation of alpha-aminoadipate. We have determined the crystal structures of LysX and its complex with ADP at 2.0A and 2.38A resolutions, respectively. LysX is composed of three alpha+beta domains, each composed of a four to five-stranded beta-sheet core flanked by alpha-helices. The C-terminal and central domains form an ATP-grasp fold, which is responsible for ATP binding. LysX has two flexible loop regions, which are expected to play an important role in substrate binding and protection. In spite of the low level of sequence identity, the overall fold of LysX is surprisingly similar to that of other ATP-grasp fold proteins, such as D-Ala:D-Ala ligase, PurT-encoded glycinamide ribonucleotide transformylase, glutathione synthetase, and synapsin I. In particular, they share a similar spatial arrangement of the amino acid residues around the ATP-binding site. This observation strongly suggests that LysX is an ATP-utilizing enzyme that shares a common evolutionary ancestor with other ATP-grasp fold proteins possessing a carboxylate-amine/thiol ligase activity.
 ==About this Structure==
-UC8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UC8 OCA].
+UC8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1UC8 OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Matsuura, T.]]
 [[Category: Nishiyama, M.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Sakai, H.]]
 [[Category: Sekine, S.]]
 [[Category: Shirouzu, M.]]
 [[Category: Terada, T.]]
-[[Category: Vassylyev, D.G.]]
+[[Category: Vassylyev, D G.]]
-[[Category: Vassylyeva, M.N.]]
+[[Category: Vassylyeva, M N.]]
 [[Category: Yokoyama, S.]]
 [[Category: alpha-aminoadipate pathway]]
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 [[Category: structural genomics]]
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