1t8p
From Proteopedia
(New page: 200px<br /> <applet load="1t8p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t8p, resolution 2.5Å" /> '''Crystal structure of...) |
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caption="1t8p, resolution 2.5Å" /> | caption="1t8p, resolution 2.5Å" /> | ||
'''Crystal structure of Human erythrocyte 2,3-bisphosphoglycerate mutase'''<br /> | '''Crystal structure of Human erythrocyte 2,3-bisphosphoglycerate mutase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bisphosphoglycerate mutase is a trifunctional enzyme of which the main | + | Bisphosphoglycerate mutase is a trifunctional enzyme of which the main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin. The gene coding for bisphosphoglycerate mutase from the human cDNA library was cloned and expressed in Escherichia coli. The protein crystals were obtained and diffract to 2.5 A and produced the first crystal structure of bisphosphoglycerate mutase. The model was refined to a crystallographic R-factor of 0.200 and R(free) of 0.266 with excellent stereochemistry. The enzyme remains a dimer in the crystal. The overall structure of the enzyme resembles that of the cofactor-dependent phosphoglycerate mutase except the regions of 13-21, 98-117, 127-151, and the C-terminal tail. The conformational changes in the backbone and the side chains of some residues reveal the structural basis for the different activities between phosphoglycerate mutase and bisphosphoglycerate mutase. The bisphosphoglycerate mutase-specific residue Gly-14 may cause the most important conformational changes, which makes the side chain of Glu-13 orient toward the active site. The positions of Glu-13 and Phe-22 prevent 2,3-bisphosphoglycerate from binding in the way proposed previously. In addition, the side chain of Glu-13 would affect the Glu-89 protonation ability responsible for the low mutase activity. Other structural variations, which could be connected with functional differences, are also discussed. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1T8P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Bisphosphoglycerate_mutase Bisphosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.4 5.4.2.4] Full crystallographic information is available from [http:// | + | 1T8P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Bisphosphoglycerate_mutase Bisphosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.4 5.4.2.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T8P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: isomerase]] | [[Category: isomerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:06 2008'' |
Revision as of 13:11, 21 February 2008
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Crystal structure of Human erythrocyte 2,3-bisphosphoglycerate mutase
Contents |
Overview
Bisphosphoglycerate mutase is a trifunctional enzyme of which the main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin. The gene coding for bisphosphoglycerate mutase from the human cDNA library was cloned and expressed in Escherichia coli. The protein crystals were obtained and diffract to 2.5 A and produced the first crystal structure of bisphosphoglycerate mutase. The model was refined to a crystallographic R-factor of 0.200 and R(free) of 0.266 with excellent stereochemistry. The enzyme remains a dimer in the crystal. The overall structure of the enzyme resembles that of the cofactor-dependent phosphoglycerate mutase except the regions of 13-21, 98-117, 127-151, and the C-terminal tail. The conformational changes in the backbone and the side chains of some residues reveal the structural basis for the different activities between phosphoglycerate mutase and bisphosphoglycerate mutase. The bisphosphoglycerate mutase-specific residue Gly-14 may cause the most important conformational changes, which makes the side chain of Glu-13 orient toward the active site. The positions of Glu-13 and Phe-22 prevent 2,3-bisphosphoglycerate from binding in the way proposed previously. In addition, the side chain of Glu-13 would affect the Glu-89 protonation ability responsible for the low mutase activity. Other structural variations, which could be connected with functional differences, are also discussed.
Disease
Known disease associated with this structure: Hemolytic anemia due to bisphosphoglycerate mutase deficiency OMIM:[222800]
About this Structure
1T8P is a Single protein structure of sequence from Homo sapiens. Active as Bisphosphoglycerate mutase, with EC number 5.4.2.4 Full crystallographic information is available from OCA.
Reference
Crystal structure of human bisphosphoglycerate mutase., Wang Y, Wei Z, Bian Q, Cheng Z, Wan M, Liu L, Gong W, J Biol Chem. 2004 Sep 10;279(37):39132-8. Epub 2004 Jul 16. PMID:15258155
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Categories: Bisphosphoglycerate mutase | Homo sapiens | Single protein | Bian, Q. | Cheng, Z. | Gong, W. | Liu, L. | Wan, M. | Wang, Y. | Wei, Z. | Isomerase
