1urr: Difference between revisions

Line 4:

==Overview==

Analysis of the Drosophila melanogaster EST database led to the discovery, and cloning of a novel acylphosphatase. The CG18505 gene coding for a new, enzyme (AcPDro2) is clearly distinct from the previously described, CG16870Acyp gene, which also codes for a D. melanogaster acylphosphatase, (AcPDro). The putative catalytic residues, together with residues held to, stabilize the acylphosphatase fold, are conserved in the two encoded, proteins. Crystals of AcPDro2, which belong to the trigonal space group, P3(1)21, with unit-cell parameters a = b = 45.8, c = 98.6 angstroms, gamma, = 120 degrees, allowed the solution of the protein structure by molecular, replacement and its refinement to 1.5 angstroms resolution. The AcPDro2, active-site structure is discussed.

Analysis of the Drosophila melanogaster EST database led to the discovery and cloning of a novel acylphosphatase. The CG18505 gene coding for a new enzyme (AcPDro2) is clearly distinct from the previously described CG16870Acyp gene, which also codes for a D. melanogaster acylphosphatase (AcPDro). The putative catalytic residues, together with residues held to stabilize the acylphosphatase fold, are conserved in the two encoded proteins. Crystals of AcPDro2, which belong to the trigonal space group P3(1)21, with unit-cell parameters a = b = 45.8, c = 98.6 angstroms, gamma = 120 degrees, allowed the solution of the protein structure by molecular replacement and its refinement to 1.5 angstroms resolution. The AcPDro2 active-site structure is discussed.

==About this Structure==

Line 21:

[[Category: enzyme]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun~~ Feb ~~3 10~~:04:11 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:34 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-Analysis of the Drosophila melanogaster EST database led to the discovery, and cloning of a novel acylphosphatase. The CG18505 gene coding for a new, enzyme (AcPDro2) is clearly distinct from the previously described, CG16870Acyp gene, which also codes for a D. melanogaster acylphosphatase, (AcPDro). The putative catalytic residues, together with residues held to, stabilize the acylphosphatase fold, are conserved in the two encoded, proteins. Crystals of AcPDro2, which belong to the trigonal space group, P3(1)21, with unit-cell parameters a = b = 45.8, c = 98.6 angstroms, gamma, = 120 degrees, allowed the solution of the protein structure by molecular, replacement and its refinement to 1.5 angstroms resolution. The AcPDro2, active-site structure is discussed.
+Analysis of the Drosophila melanogaster EST database led to the discovery and cloning of a novel acylphosphatase. The CG18505 gene coding for a new enzyme (AcPDro2) is clearly distinct from the previously described CG16870Acyp gene, which also codes for a D. melanogaster acylphosphatase (AcPDro). The putative catalytic residues, together with residues held to stabilize the acylphosphatase fold, are conserved in the two encoded proteins. Crystals of AcPDro2, which belong to the trigonal space group P3(1)21, with unit-cell parameters a = b = 45.8, c = 98.6 angstroms, gamma = 120 degrees, allowed the solution of the protein structure by molecular replacement and its refinement to 1.5 angstroms resolution. The AcPDro2 active-site structure is discussed.
 ==About this Structure==
@@ Line 21: / Line 21: @@
 [[Category: enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:04:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:27:34 2008''