1dof
From Proteopedia
(New page: 200px<br /><applet load="1dof" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dof, resolution 2.10Å" /> '''THE CRYSTAL STRUCTUR...) |
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| - | [[Image:1dof.gif|left|200px]]<br /><applet load="1dof" size=" | + | [[Image:1dof.gif|left|200px]]<br /><applet load="1dof" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dof, resolution 2.10Å" /> | caption="1dof, resolution 2.10Å" /> | ||
'''THE CRYSTAL STRUCTURE OF ADENYLOSUCCINATE LYASE FROM PYROBACULUM AEROPHILUM: INSIGHTS INTO THERMAL STABILITY AND HUMAN PATHOLOGY'''<br /> | '''THE CRYSTAL STRUCTURE OF ADENYLOSUCCINATE LYASE FROM PYROBACULUM AEROPHILUM: INSIGHTS INTO THERMAL STABILITY AND HUMAN PATHOLOGY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Adenylosuccinate lyase catalyzes two separate reactions in the de novo | + | Adenylosuccinate lyase catalyzes two separate reactions in the de novo purine biosynthetic pathway. Through its dual action in this pathway, adenylosuccinate lyase plays an integral part in cellular replication and metabolism. Mutations in the human enzyme can result in severe neurological disorders, including mental retardation with autistic features. The crystal structure of adenylosuccinate lyase from the hyperthermophilic archaebacterium Pyrobaculum aerophilum has been determined to 2.1 A resolution. Although both the fold of the monomer and the architecture of the tetrameric assembly are similar to adenylosuccinate lyase from the thermophilic eubacterium Thermotoga maritima, the archaebacterial lyase contains unique features. Surprisingly, the structure of adenylosuccinate lyase from P. aerophilum reveals that this intracellular protein contains three disulfide bonds that contribute significantly to its stability against thermal and chemical denaturation. The observation of multiple disulfide bonds in the recombinant form of the enzyme suggests the need for further investigations into whether the intracellular environment of P. aerophilum, and possibly other hyperthermophiles, may be compatible with protein disulfide bond formation. In addition, the protein is shorter in P. aerophilum than it is in other organisms. This abbreviation results from an internal excision of a cluster of helices that may be involved in protein-protein interactions in other organisms and may relate to the observed clinical effects of human mutations in that region. |
==About this Structure== | ==About this Structure== | ||
| - | 1DOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Active as [http://en.wikipedia.org/wiki/Adenylosuccinate_lyase Adenylosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.2 4.3.2.2] Full crystallographic information is available from [http:// | + | 1DOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Active as [http://en.wikipedia.org/wiki/Adenylosuccinate_lyase Adenylosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.2 4.3.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pyrobaculum aerophilum]] | [[Category: Pyrobaculum aerophilum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dixon, J | + | [[Category: Dixon, J E.]] |
[[Category: Goedken, E.]] | [[Category: Goedken, E.]] | ||
[[Category: Marqusee, S.]] | [[Category: Marqusee, S.]] | ||
| - | [[Category: Toth, E | + | [[Category: Toth, E A.]] |
| - | [[Category: Yeates, T | + | [[Category: Yeates, T O.]] |
[[Category: lyase]] | [[Category: lyase]] | ||
[[Category: purine biosynthesis]] | [[Category: purine biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:44 2008'' |
Revision as of 10:18, 21 February 2008
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THE CRYSTAL STRUCTURE OF ADENYLOSUCCINATE LYASE FROM PYROBACULUM AEROPHILUM: INSIGHTS INTO THERMAL STABILITY AND HUMAN PATHOLOGY
Overview
Adenylosuccinate lyase catalyzes two separate reactions in the de novo purine biosynthetic pathway. Through its dual action in this pathway, adenylosuccinate lyase plays an integral part in cellular replication and metabolism. Mutations in the human enzyme can result in severe neurological disorders, including mental retardation with autistic features. The crystal structure of adenylosuccinate lyase from the hyperthermophilic archaebacterium Pyrobaculum aerophilum has been determined to 2.1 A resolution. Although both the fold of the monomer and the architecture of the tetrameric assembly are similar to adenylosuccinate lyase from the thermophilic eubacterium Thermotoga maritima, the archaebacterial lyase contains unique features. Surprisingly, the structure of adenylosuccinate lyase from P. aerophilum reveals that this intracellular protein contains three disulfide bonds that contribute significantly to its stability against thermal and chemical denaturation. The observation of multiple disulfide bonds in the recombinant form of the enzyme suggests the need for further investigations into whether the intracellular environment of P. aerophilum, and possibly other hyperthermophiles, may be compatible with protein disulfide bond formation. In addition, the protein is shorter in P. aerophilum than it is in other organisms. This abbreviation results from an internal excision of a cluster of helices that may be involved in protein-protein interactions in other organisms and may relate to the observed clinical effects of human mutations in that region.
About this Structure
1DOF is a Single protein structure of sequence from Pyrobaculum aerophilum. Active as Adenylosuccinate lyase, with EC number 4.3.2.2 Full crystallographic information is available from OCA.
Reference
The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds., Toth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO, J Mol Biol. 2000 Aug 11;301(2):433-50. PMID:10926519
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