2be9
From Proteopedia
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| - | [[Image:2be9.jpg|left|200px]] | + | [[Image:2be9.jpg|left|200px]] |
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| - | '''Crystal structure of the CTP-liganded (T-State) aspartate transcarbamoylase from the extremely thermophilic archaeon Sulfolobus acidocaldarius''' | + | {{Structure |
| + | |PDB= 2be9 |SIZE=350|CAPTION= <scene name='initialview01'>2be9</scene>, resolution 2.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CTP:CYTIDINE-5'-TRIPHOSPHATE'>CTP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] | ||
| + | |GENE= pyrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 Sulfolobus acidocaldarius]), pyrI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2285 Sulfolobus acidocaldarius]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the CTP-liganded (T-State) aspartate transcarbamoylase from the extremely thermophilic archaeon Sulfolobus acidocaldarius''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BE9 is a [ | + | 2BE9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BE9 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of T state aspartate carbamoyltransferase of the hyperthermophilic archaeon Sulfolobus acidocaldarius., De Vos D, Van Petegem F, Remaut H, Legrain C, Glansdorff N, Van Beeumen JJ, J Mol Biol. 2004 Jun 11;339(4):887-900. PMID:[http:// | + | Crystal structure of T state aspartate carbamoyltransferase of the hyperthermophilic archaeon Sulfolobus acidocaldarius., De Vos D, Van Petegem F, Remaut H, Legrain C, Glansdorff N, Van Beeumen JJ, J Mol Biol. 2004 Jun 11;339(4):887-900. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15165857 15165857] |
[[Category: Aspartate carbamoyltransferase]] | [[Category: Aspartate carbamoyltransferase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:00:45 2008'' |
Revision as of 14:00, 20 March 2008
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| , resolution 2.60Å | |||||||
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| Ligands: | , and | ||||||
| Gene: | pyrB (Sulfolobus acidocaldarius), pyrI (Sulfolobus acidocaldarius) | ||||||
| Activity: | Aspartate carbamoyltransferase, with EC number 2.1.3.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the CTP-liganded (T-State) aspartate transcarbamoylase from the extremely thermophilic archaeon Sulfolobus acidocaldarius
Overview
Aspartate carbamoyltransferase (ATCase) is a model enzyme for understanding allosteric effects. The dodecameric complex exists in two main states (T and R) that differ substantially in their quaternary structure and their affinity for various ligands. Many hypotheses have resulted from the structure of the Escherichia coli ATCase, but so far other crystal structures to test these have been lacking. Here, we present the tertiary and quaternary structure of the T state ATCase of the hyperthermophilic archaeon Sulfolobus acidocaldarius (SaATC(T)), determined by X-ray crystallography to 2.6A resolution. The quaternary structure differs from the E.coli ATCase, by having altered interfaces between the catalytic (C) and regulatory (R) subunits, and the presence of a novel C1-R2 type interface. Conformational differences in the 240 s loop region of the C chain and the C-terminal region of the R chain affect intersubunit and interdomain interfaces implicated previously in the allosteric behavior of E.coli ATCase. The allosteric-zinc binding domain interface is strengthened at the expense of a weakened R1-C4 type interface. The increased hydrophobicity of the C1-R1 type interface may stabilize the quaternary structure. Catalytic trimers of the S.acidocaldarius ATCase are unstable due to a drastic weakening of the C1-C2 interface. The hyperthermophilic ATCase presents an interesting example of how an allosteric enzyme can adapt to higher temperatures. The structural rearrangement of this thermophilic ATCase may well promote its thermal stability at the expense of changes in the allosteric behavior.
About this Structure
2BE9 is a Protein complex structure of sequences from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.
Reference
Crystal structure of T state aspartate carbamoyltransferase of the hyperthermophilic archaeon Sulfolobus acidocaldarius., De Vos D, Van Petegem F, Remaut H, Legrain C, Glansdorff N, Van Beeumen JJ, J Mol Biol. 2004 Jun 11;339(4):887-900. PMID:15165857
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