5csc
From Proteopedia
(New page: 200px<br /><applet load="5csc" size="450" color="white" frame="true" align="right" spinBox="true" caption="5csc, resolution 2.8Å" /> '''STRUCTURE OF AN OPEN ...) |
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| - | [[Image:5csc.gif|left|200px]]<br /><applet load="5csc" size=" | + | [[Image:5csc.gif|left|200px]]<br /><applet load="5csc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="5csc, resolution 2.8Å" /> | caption="5csc, resolution 2.8Å" /> | ||
'''STRUCTURE OF AN OPEN FORM OF CHICKEN HEART CITRATE SYNTHASE AT 2.8 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURE OF AN OPEN FORM OF CHICKEN HEART CITRATE SYNTHASE AT 2.8 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray structure of a new crystal form of chicken heart muscle citrate | + | The X-ray structure of a new crystal form of chicken heart muscle citrate synthase, grown from solutions containing citrate and coenzyme A or L-malate and acetyl coenzyme A, has been determined by molecular replacement at 2.8-A resolution. The space group is P4(3) with a = 58.9 A and c = 259.2 A and contains an entire dimer of molecular weight 100,000 in the asymmetric unit. Both "closed" conformation chicken heart and "open" conformation pig heart citrate synthase models (Brookhaven Protein Data Bank designations 3CTS and 1CTS) were used in the molecular replacement solution, with crystallographic refinement being initiated with the latter. The conventional crystallographic R factor of the final refined model is 19.6% for the data between 6- and 2.8-A resolution. The model has an rms deviation from ideal values of 0.034 A for bond lengths and of 3.6 degrees for bond angles. The conformation of the enzyme is essentially identical with that of a previously determined "open" form of pig heart muscle citrate synthase which crystallizes in a different space group, with one monomer in the asymmetric unit, from either phosphate or citrate solution. The crystalline environment of each subunit of the chicken enzyme is different, yet the conformation is the same in each. The open conformation is therefore not an artifact of crystal packing or crystallization conditions and is not species dependent. Both "open" and "closed" crystal forms of the chicken heart enzyme grow from the same drop, showing that both conformations of the enzyme are present at equilibrium in solution containing reaction products or substrate analogues. |
==About this Structure== | ==About this Structure== | ||
| - | 5CSC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1] Full crystallographic information is available from [http:// | + | 5CSC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CSC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Karpusas, M.]] | [[Category: Karpusas, M.]] | ||
| - | [[Category: Liao, D | + | [[Category: Liao, D I.]] |
| - | [[Category: Remington, S | + | [[Category: Remington, S J.]] |
[[Category: oxo-acid-lyase]] | [[Category: oxo-acid-lyase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:04 2008'' |
Revision as of 17:15, 21 February 2008
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STRUCTURE OF AN OPEN FORM OF CHICKEN HEART CITRATE SYNTHASE AT 2.8 ANGSTROMS RESOLUTION
Overview
The X-ray structure of a new crystal form of chicken heart muscle citrate synthase, grown from solutions containing citrate and coenzyme A or L-malate and acetyl coenzyme A, has been determined by molecular replacement at 2.8-A resolution. The space group is P4(3) with a = 58.9 A and c = 259.2 A and contains an entire dimer of molecular weight 100,000 in the asymmetric unit. Both "closed" conformation chicken heart and "open" conformation pig heart citrate synthase models (Brookhaven Protein Data Bank designations 3CTS and 1CTS) were used in the molecular replacement solution, with crystallographic refinement being initiated with the latter. The conventional crystallographic R factor of the final refined model is 19.6% for the data between 6- and 2.8-A resolution. The model has an rms deviation from ideal values of 0.034 A for bond lengths and of 3.6 degrees for bond angles. The conformation of the enzyme is essentially identical with that of a previously determined "open" form of pig heart muscle citrate synthase which crystallizes in a different space group, with one monomer in the asymmetric unit, from either phosphate or citrate solution. The crystalline environment of each subunit of the chicken enzyme is different, yet the conformation is the same in each. The open conformation is therefore not an artifact of crystal packing or crystallization conditions and is not species dependent. Both "open" and "closed" crystal forms of the chicken heart enzyme grow from the same drop, showing that both conformations of the enzyme are present at equilibrium in solution containing reaction products or substrate analogues.
About this Structure
5CSC is a Single protein structure of sequence from Gallus gallus. Active as Citrate (Si)-synthase, with EC number 2.3.3.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of an open conformation of citrate synthase from chicken heart at 2.8-A resolution., Liao DI, Karpusas M, Remington SJ, Biochemistry. 1991 Jun 18;30(24):6031-6. PMID:2043641
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