1ibv
From Proteopedia
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| - | [[Image:1ibv.jpg|left|200px]] | + | [[Image:1ibv.jpg|left|200px]] |
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| - | '''STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT-170 C''' | + | {{Structure |
| + | |PDB= 1ibv |SIZE=350|CAPTION= <scene name='initialview01'>1ibv</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PVH:HISTIDINE-METHYL-ESTER'>PVH</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= HDCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1591 Lactobacillus sp.]) | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT-170 C''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IBV is a [ | + | 1IBV is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Lactobacillus_sp. Lactobacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBV OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a., Worley S, Schelp E, Monzingo AF, Ernst S, Robertus JD, Proteins. 2002 Feb 15;46(3):321-9. PMID:[http:// | + | Structure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a., Worley S, Schelp E, Monzingo AF, Ernst S, Robertus JD, Proteins. 2002 Feb 15;46(3):321-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11835507 11835507] |
[[Category: Histidine decarboxylase]] | [[Category: Histidine decarboxylase]] | ||
[[Category: Lactobacillus sp.]] | [[Category: Lactobacillus sp.]] | ||
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[[Category: substrate-induced activation]] | [[Category: substrate-induced activation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:48:17 2008'' |
Revision as of 09:48, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Gene: | HDCA (Lactobacillus sp.) | ||||||
| Activity: | Histidine decarboxylase, with EC number 4.1.1.22 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE BOUND WITH HISTIDINE METHYL ESTER AT-170 C
Overview
Histidine decarboxylase (HDC) from Lactobacillus 30a converts histidine to histamine, a process that enables the bacteria to maintain the optimum pH range for cell growth. HDC is regulated by pH; it is active at low pH and inactive at neutral to alkaline pH. The X-ray structure of HDC at pH 8 revealed that a helix was disordered, resulting in the disruption of the substrate-binding site. The HDC trimer has also been shown to exhibit cooperative kinetics at neutral pH, that is, histidine can trigger a T-state to R-state transition. The D53,54N mutant of HDC has an elevated Km, even at low pH, indicating that the enzyme assumes the low activity T-state. We have solved the structures of the D53,54N mutant at low pH, with and without the substrate analog histidine methyl ester (HME) bound. Structural analysis shows that the apo-D53,54N mutant is in the inactive or T-state and that binding of the substrate analog induces the enzyme to adopt the active or R-state. A mechanism for the cooperative transition is proposed.
About this Structure
1IBV is a Protein complex structure of sequences from Lactobacillus sp.. Full crystallographic information is available from OCA.
Reference
Structure and cooperativity of a T-state mutant of histidine decarboxylase from Lactobacillus 30a., Worley S, Schelp E, Monzingo AF, Ernst S, Robertus JD, Proteins. 2002 Feb 15;46(3):321-9. PMID:11835507
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