1hq6
From Proteopedia
(New page: 200px<br /><applet load="1hq6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hq6, resolution 2.7Å" /> '''STRUCTURE OF PYRUVOYL...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hq6.jpg|left|200px]]<br /><applet load="1hq6" size=" | + | [[Image:1hq6.jpg|left|200px]]<br /><applet load="1hq6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hq6, resolution 2.7Å" /> | caption="1hq6, resolution 2.7Å" /> | ||
'''STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8'''<br /> | '''STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Histidine decarboxylase (HDC) from Lactobacillus 30a produces histamine | + | Histidine decarboxylase (HDC) from Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism of pH regulation. At high pH helix B is unwound, destroying the substrate binding pocket. At acid pH the helix is stabilized, partly through protonation of Asp198 and Asp53 on either side of the molecular interface, acting as a proton trap. In contrast to hemoglobin regulation, pH has a large effect on the tertiary structure of HDC monomers and relatively little or no effect on quaternary structure. |
==About this Structure== | ==About this Structure== | ||
| - | 1HQ6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Lactobacillus_sp. Lactobacillus sp.]. Active as [http://en.wikipedia.org/wiki/Histidine_decarboxylase Histidine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.22 4.1.1.22] Full crystallographic information is available from [http:// | + | 1HQ6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Lactobacillus_sp. Lactobacillus sp.]. Active as [http://en.wikipedia.org/wiki/Histidine_decarboxylase Histidine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.22 4.1.1.22] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQ6 OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ernst, S.]] | [[Category: Ernst, S.]] | ||
| - | [[Category: Monzingo, A | + | [[Category: Monzingo, A F.]] |
| - | [[Category: Robertus, J | + | [[Category: Robertus, J D.]] |
[[Category: Schelp, E.]] | [[Category: Schelp, E.]] | ||
[[Category: Worley, S.]] | [[Category: Worley, S.]] | ||
| Line 25: | Line 25: | ||
[[Category: pyruvoyl]] | [[Category: pyruvoyl]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:43 2008'' |
Revision as of 11:03, 21 February 2008
|
STRUCTURE OF PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE AT PH 8
Overview
Histidine decarboxylase (HDC) from Lactobacillus 30a produces histamine that is essential to counter waste acids, and to optimize cell growth. The HDC trimer is active at low pH and inactive at neutral to alkaline pH. We have solved the X-ray structure of HDC at pH 8 and revealed the novel mechanism of pH regulation. At high pH helix B is unwound, destroying the substrate binding pocket. At acid pH the helix is stabilized, partly through protonation of Asp198 and Asp53 on either side of the molecular interface, acting as a proton trap. In contrast to hemoglobin regulation, pH has a large effect on the tertiary structure of HDC monomers and relatively little or no effect on quaternary structure.
About this Structure
1HQ6 is a Protein complex structure of sequences from Lactobacillus sp.. Active as Histidine decarboxylase, with EC number 4.1.1.22 Full crystallographic information is available from OCA.
Reference
pH-induced structural changes regulate histidine decarboxylase activity in Lactobacillus 30a., Schelp E, Worley S, Monzingo AF, Ernst S, Robertus JD, J Mol Biol. 2001 Mar 2;306(4):727-32. PMID:11243783
Page seeded by OCA on Thu Feb 21 13:03:43 2008
