1hn1
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1hn1 |SIZE=350|CAPTION= <scene name='initialview01'>1hn1</scene>, resolution 3.0Å | |PDB= 1hn1 |SIZE=350|CAPTION= <scene name='initialview01'>1hn1</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA_thioesterase 4-hydroxybenzoyl-CoA thioesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.23 3.1.2.23] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA_thioesterase 4-hydroxybenzoyl-CoA thioesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.23 3.1.2.23] </span> |
|GENE= LAC Z ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= LAC Z ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1f4h|1F4H]], [[1dp0|1DP0]], [[1f4a|1F4A]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn1 OCA], [http://www.ebi.ac.uk/pdbsum/1hn1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hn1 RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Juers, D H.]] | [[Category: Juers, D H.]] | ||
[[Category: Matthews, B W.]] | [[Category: Matthews, B W.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NA]] | ||
[[Category: alpha/beta barrel]] | [[Category: alpha/beta barrel]] | ||
[[Category: beta supersandwich]] | [[Category: beta supersandwich]] | ||
| Line 32: | Line 33: | ||
[[Category: jelly roll barrel]] | [[Category: jelly roll barrel]] | ||
| - | ''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 21:07:55 2008'' |
Revision as of 18:07, 30 March 2008
| |||||||
| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | LAC Z (Escherichia coli) | ||||||
| Activity: | 4-hydroxybenzoyl-CoA thioesterase, with EC number 3.1.2.23 | ||||||
| Related: | 1F4H, 1DP0, 1F4A
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
E. COLI (LAC Z) BETA-GALACTOSIDASE (ORTHORHOMBIC)
Overview
Flash-freezing, which has become routine in macromolecular X-ray crystallography, causes the crystal to contract substantially. In the case of Escherichia coli beta-galactosidase the changes are reversible and are shown to be due to lattice repacking. On cooling, the area of the protein surface involved in lattice contacts increases by 50 %. There are substantial alterations in intermolecular contacts, these changes being dominated by the long, polar side-chains. For entropic reasons such side-chains, as well as surface solvent molecules, tend to be somewhat disordered at room temperature but can form extensive hydrogen-bonded networks on cooling. Low-temperature density measurements suggest that, at least in some cases, the beneficial effect of cryosolvents may be due to a density increase on vitrification which reduces the volume of bulk solvent that needs to be expelled from the crystal. Analysis of beta-galactosidase and several other proteins suggests that both intramolecular and intermolecular contact interfaces can be perturbed by cryocooling but that the changes tend to be more dramatic in the latter case. The temperature-dependence of the intermolecular interactions suggests that caution may be necessary in interpreting protein-protein and protein-nucleic acid interactions based on low-temperature crystal structures.
About this Structure
1HN1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Reversible lattice repacking illustrates the temperature dependence of macromolecular interactions., Juers DH, Matthews BW, J Mol Biol. 2001 Aug 24;311(4):851-62. PMID:11518535
Page seeded by OCA on Sun Mar 30 21:07:55 2008
