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1ibv
From Proteopedia
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|PDB= 1ibv |SIZE=350|CAPTION= <scene name='initialview01'>1ibv</scene>, resolution 2.5Å | |PDB= 1ibv |SIZE=350|CAPTION= <scene name='initialview01'>1ibv</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PVH:HISTIDINE-METHYL-ESTER'>PVH</scene> | + | |LIGAND= <scene name='pdbligand=PVH:HISTIDINE-METHYL-ESTER'>PVH</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= HDCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1591 Lactobacillus sp.]) | |GENE= HDCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1591 Lactobacillus sp.]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1pya|1PYA]], [[1hq6|1HQ6]], [[1ibt|1IBT]], [[1ibu|1IBU]], [[1ibw|1IBW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ibv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibv OCA], [http://www.ebi.ac.uk/pdbsum/1ibv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ibv RCSB]</span> | ||
}} | }} | ||
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[[Category: Schelp, E.]] | [[Category: Schelp, E.]] | ||
[[Category: Worley, S.]] | [[Category: Worley, S.]] | ||
| - | [[Category: PVH]] | ||
[[Category: active form]] | [[Category: active form]] | ||
[[Category: carboxy-lyase]] | [[Category: carboxy-lyase]] | ||
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[[Category: substrate-induced activation]] | [[Category: substrate-induced activation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:17:34 2008'' |
Revision as of 18:17, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | HDCA (Lactobacillus sp.) | ||||||
| Activity: | Histidine decarboxylase, with EC number 4.1.1.22 | ||||||
| Related: | 1PYA, 1HQ6, 1IBT, 1IBU, 1IBW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 21:17:34 2008
