1pda
From Proteopedia
(New page: 200px<br /><applet load="1pda" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pda, resolution 1.76Å" /> '''STRUCTURE OF PORPHOB...) |
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| - | [[Image:1pda.jpg|left|200px]]<br /><applet load="1pda" size=" | + | [[Image:1pda.jpg|left|200px]]<br /><applet load="1pda" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pda, resolution 1.76Å" /> | caption="1pda, resolution 1.76Å" /> | ||
'''STRUCTURE OF PORPHOBILINOGEN DEAMINASE REVEALS A FLEXIBLE MULTIDOMAIN POLYMERASE WITH A SINGLE CATALYTIC SITE'''<br /> | '''STRUCTURE OF PORPHOBILINOGEN DEAMINASE REVEALS A FLEXIBLE MULTIDOMAIN POLYMERASE WITH A SINGLE CATALYTIC SITE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-domain structure of porphobilinogen deaminase, a key enzyme in | + | The three-domain structure of porphobilinogen deaminase, a key enzyme in the biosynthetic pathway of tetrapyrroles, has been defined by X-ray analysis at 1.9 A resolution. Two of the domains structurally resemble the transferrins and periplasmic binding proteins. The dipyrromethane cofactor is covalently linked to domain 3 but is bound by extensive salt-bridges and hydrogen-bonds within the cleft between domains 1 and 2, at a position corresponding to the binding sites for small-molecule ligands in the analogous proteins. The X-ray structure and results from site-directed mutagenesis provide evidence for a single catalytic site. Interdomain flexibility may aid elongation of the polypyrrole product in the active-site cleft of the enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1PDA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with DPM and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydroxymethylbilane_synthase Hydroxymethylbilane synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.61 2.5.1.61] Full crystallographic information is available from [http:// | + | 1PDA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=DPM:'>DPM</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydroxymethylbilane_synthase Hydroxymethylbilane synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.61 2.5.1.61] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PDA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hydroxymethylbilane synthase]] | [[Category: Hydroxymethylbilane synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blundell, T | + | [[Category: Blundell, T L.]] |
| - | [[Category: Brownlie, P | + | [[Category: Brownlie, P D.]] |
| - | [[Category: Cooper, J | + | [[Category: Cooper, J B.]] |
| - | [[Category: Jordan, P | + | [[Category: Jordan, P M.]] |
[[Category: Lambert, R.]] | [[Category: Lambert, R.]] | ||
| - | [[Category: Louie, G | + | [[Category: Louie, G V.]] |
| - | [[Category: Warren, M | + | [[Category: Warren, M J.]] |
| - | [[Category: Wood, S | + | [[Category: Wood, S P.]] |
| - | [[Category: Woodcock, S | + | [[Category: Woodcock, S C.]] |
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: DPM]] | [[Category: DPM]] | ||
[[Category: lyase(porphyrin)]] | [[Category: lyase(porphyrin)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:38 2008'' |
Revision as of 12:27, 21 February 2008
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STRUCTURE OF PORPHOBILINOGEN DEAMINASE REVEALS A FLEXIBLE MULTIDOMAIN POLYMERASE WITH A SINGLE CATALYTIC SITE
Overview
The three-domain structure of porphobilinogen deaminase, a key enzyme in the biosynthetic pathway of tetrapyrroles, has been defined by X-ray analysis at 1.9 A resolution. Two of the domains structurally resemble the transferrins and periplasmic binding proteins. The dipyrromethane cofactor is covalently linked to domain 3 but is bound by extensive salt-bridges and hydrogen-bonds within the cleft between domains 1 and 2, at a position corresponding to the binding sites for small-molecule ligands in the analogous proteins. The X-ray structure and results from site-directed mutagenesis provide evidence for a single catalytic site. Interdomain flexibility may aid elongation of the polypyrrole product in the active-site cleft of the enzyme.
About this Structure
1PDA is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Hydroxymethylbilane synthase, with EC number 2.5.1.61 Full crystallographic information is available from OCA.
Reference
Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site., Louie GV, Brownlie PD, Lambert R, Cooper JB, Blundell TL, Wood SP, Warren MJ, Woodcock SC, Jordan PM, Nature. 1992 Sep 3;359(6390):33-9. PMID:1522882
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