 |
|
|
 |
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
197 a.a.
_CA
Key reference
DOI no: 10.1107/S0907444900003334 Acta Crystallogr D Biol Crystallogr 56:749-750 (2000) PubMed id: 10818352
Crystallization and preliminary X-ray analysis of high-alkaline pectate lyase. M.Akita, A.Suzuki, T.Kobayashi, S.Ito, T.Yamane. ABSTRACT
Pel-15, a high-alkaline pectate lyase (pectate transeliminase; E.C. 4.2.2.2) from Bacillus sp. strain KSM-P15, has been crystallized using the hanging-drop vapour-diffusion method at 277 K. Two different crystal forms were obtained and preliminary X-ray diffraction data were collected from each crystal form at 100 K. Both forms belong to the orthorhombic space group P2(1)2(1)2(1) and contain one molecule per asymmetric unit. The unit-cell parameters of form I are a = 43.2 (2), b = 60.2 (2), c = 82.2 (2) A and those of form II are a = 42.9 (1), b = 43.4 (1), c = 105.9 (3) A. Diffraction data to a resolution of 1.5 A were collected from form II crystals using a synchrotron-radiation source.
Selected figure(s)
Figure 1.
Figure 1 Crystals of Pel-15 grown in 28%(w/v) PEG 8000 in 100 mM MES-NaOH pH 6.7 buffer.The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 749-750) copyright 2000. Figure was selected by an automated process.
Added reference
DOI no: 10.1107/S0907444901014482 Acta Crystallogr D Biol Crystallogr 57:1786-1792 (2001) PubMed id: 11717490
The first structure of pectate lyase belonging to polysaccharide lyase family 3. M.Akita, A.Suzuki, T.Kobayashi, S.Ito, T.Yamane. ABSTRACT
Pel-15, a high-alkaline pectate lyase (pectate transeliminase; E.C. 4.2.2.2) from Bacillus sp. strain KSM-P15, has been crystallized using the hanging-drop vapour-diffusion method at 277 K. Two different crystal forms were obtained and preliminary X-ray diffraction data were collected from each crystal form at 100 K. Both forms belong to the orthorhombic space group P2(1)2(1)2(1) and contain one molecule per asymmetric unit. The unit-cell parameters of form I are a = 43.2 (2), b = 60.2 (2), c = 82.2 (2) A and those of form II are a = 42.9 (1), b = 43.4 (1), c = 105.9 (3) A. Diffraction data to a resolution of 1.5 A were collected from form II crystals using a synchrotron-radiation source.
Selected figure(s)
Figure 3.
Figure 3 Stereoview of the Pel-15 unique calcium-binding site formed by Asp80, Val81, Lys103 and three water molecules. One calcium-bound water molecule is bound to the O atom of Gly34 on the first T3. The location of this region is shown in Fig. 1-.Figure 5.
Figure 5 Stereoviews of the T3-PB1 groove regions of (a) Pel-15 and (b) Ech-PelC (PDB entry [202]1air ). The location of this region is shown in Fig. 1[203] [link]-[204][turqarr.gif] . Amino-acid side chains are represented by stick models. The calcium ion and amino-acid side chains in the pH 9.5 structure are represented by a yellow sphere and red sticks, respectively. The conformations of those amino-acid side chains are changed by attachment of the calcium ion.The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 1786-1792) copyright 2001. Figures were selected by an automated process.
 |
 |