Crystallization and preliminary X-ray diffraction analysis of human seminal plasma protein PSP94.
نویسندگان
چکیده
The human seminal plasma protein PSP94 is a small protein of 94 residues that contains ten cysteines. Since its discovery about 25 years ago, several potential biological functions have been reported for this protein. Many PSP94 homologues have also been identified since then from various species, but no crystal structure has been determined to date. PSP94 has been purified from human seminal plasma and crystallized. These crystals diffracted to approximately 2.3 A resolution and belonged to space group P4(1)2(1)2, with unit-cell parameters a = 107.9, b = 107.9, c = 92.1 A. There are four molecules in the asymmetric unit. Structure solution by the heavy-atom method is currently in progress.
منابع مشابه
Prostate Secretory Protein of 94 Amino Acids (PSP94) Binds to Prostatic Acid Phosphatase (PAP) in Human Seminal Plasma
Prostate Secretory Protein of 94 amino acids (PSP94) is one of the major proteins present in the human seminal plasma. Though several functions have been predicted for this protein, its exact role either in sperm function or in prostate pathophysiology has not been clearly defined. Attempts to understand the mechanism of action of PSP94 has led to the search for its probable binding partners. T...
متن کاملCrystallization and preliminary X-ray crystallographic analysis of human plasma platelet activating factor acetylhydrolase.
The plasma form of the human enzyme platelet activating factor acetylhydrolase (PAF-AH) has been crystallized, and X-ray diffraction data were collected at a synchrotron source to a resolution of 1.47 A. The crystals belong to space group C2, with unit cell parameters of a = 116.18, b = 83.06, c = 96.71 A, and beta= 115.09 degrees and two molecules in the asymmetric unit. PAF-AH functions as a ...
متن کاملStructural and molecular biology of PSP94: Its significance in prostate pathophysiology.
Prostate secretory protein of 94 amino acids (PSP94), primarily found in the prostatic secretion, was originally isolated and purified from human seminal plasma. PSP94 has several putative biological functions and is considered a marker of prostate cancer (PCa). Here, we review the structural-functional relationships of PSP94, address its fungicidal activity and role as an inhibitor of sperm mo...
متن کاملExpression, purification, crystallization and preliminary X-ray diffraction analysis of the novel modular DNA-binding protein BurrH in its apo form and in complex with its target DNA.
Different genome-editing strategies have fuelled the development of new DNA-targeting molecular tools allowing precise gene modifications. Here, the expression, purification, crystallization and preliminary X-ray diffraction of BurrH, a novel DNA-binding protein from Burkholderia rhizoxinica, are reported. Crystallization experiments of BurrH in its apo form and in complex with its target DNA y...
متن کاملCrystallization and preliminary X-ray diffraction studies of a surface mutant of the middle domain of PB2 from human influenza A (H1N1) virus.
In the last hundred years, four influenza pandemics have been experienced, beginning with that in Spain in 1918. Influenza A virus causes severe pneumonia and its RNA polymerase is an important target for drug design. The influenza A (H1N1) virus has eight ribonucleoprotein complexes, which are composed of viral RNA, RNA polymerases and nucleoproteins. PB2 forms part of the RNA polymerase compl...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Acta crystallographica. Section F, Structural biology and crystallization communications
دوره 65 Pt 4 شماره
صفحات -
تاریخ انتشار 2009