1hqs: Difference between revisions
New page: left|200px<br /><applet load="1hqs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hqs, resolution 1.55Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1hqs.gif|left|200px]]<br /><applet load="1hqs" size=" | [[Image:1hqs.gif|left|200px]]<br /><applet load="1hqs" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1hqs, resolution 1.55Å" /> | caption="1hqs, resolution 1.55Å" /> | ||
'''CRYSTAL STRUCTURE OF ISOCITRATE DEHYDROGENASE FROM BACILLUS SUBTILIS'''<br /> | '''CRYSTAL STRUCTURE OF ISOCITRATE DEHYDROGENASE FROM BACILLUS SUBTILIS'''<br /> | ||
==Overview== | ==Overview== | ||
Isocitrate dehydrogenase from Bacillus subtilis (BsIDH) is a member of a | Isocitrate dehydrogenase from Bacillus subtilis (BsIDH) is a member of a family of metal-dependent decarboxylating dehydrogenases. Its crystal structure was solved to 1.55 A and detailed comparisons with the homologue from Escherichia coli (EcIDH), the founding member of this family, were made. Although the two IDHs are structurally similar, there are three notable differences between them. First, a mostly nonpolar beta-strand and two connecting loops in the small domain of EcIDH are replaced by two polar alpha-helices in BsIDH. Because of a 13-residue insert in this region of BsIDH, these helices protrude over the active site cleft of the opposing monomer. Second, a coil leading into this cleft, the so-called "phosphorylation" loop, is bent inward in the B. subtilis enzyme, narrowing the entrance to the active site from about 12 to 4 A. Third, although BsIDH is a homodimer, the two unique crystallographic subunits of BsIDH are not structurally identical. The two monomers appear to differ by a domain shift of the large domain relative to the small domain/clasp region, reminiscent of what has been observed in the open/closed conformations of EcIDH. In Escherichia coli, IDH is regulated by reversible phosphorylation by the bifunctional enzyme IDH kinase/phosphatase (IDH-K/P). The site of phosphorylation is Ser(113), which lies deep within the active site crevice. Structural differences between EcIDH and BsIDH may explain disparities in their abilities to act as substrates for IDH-K/P. | ||
==About this Structure== | ==About this Structure== | ||
1HQS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with CIT, PGO and PGR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] Full crystallographic information is available from [http:// | 1HQS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=CIT:'>CIT</scene>, <scene name='pdbligand=PGO:'>PGO</scene> and <scene name='pdbligand=PGR:'>PGR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQS OCA]. | ||
==Reference== | ==Reference== | ||
Line 14: | Line 14: | ||
[[Category: Isocitrate dehydrogenase (NADP(+))]] | [[Category: Isocitrate dehydrogenase (NADP(+))]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Banaszak, L | [[Category: Banaszak, L J.]] | ||
[[Category: LaPorte, D | [[Category: LaPorte, D C.]] | ||
[[Category: Matsuno, K.]] | [[Category: Matsuno, K.]] | ||
[[Category: Singh, S | [[Category: Singh, S K.]] | ||
[[Category: CIT]] | [[Category: CIT]] | ||
[[Category: PGO]] | [[Category: PGO]] | ||
Line 28: | Line 28: | ||
[[Category: tricarboxylic acid cycle]] | [[Category: tricarboxylic acid cycle]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:54 2008'' |