XYLOSE ISOMERASE FROM THERMOTOGA NEAPOLITANA

Crystal Structures of Class II Xylose Isomerases from Two Thermophiles and a Hyperthermophile

Crystallization and Initial X-Ray Analysis of Xylose Isomerase from Thermotoga Neapolitana

Xyla Cloning and Sequencing and Biochemical Characterization of Xylose Isomerase from Thermotoga Neapolitana

AEFFPEIPKVQFEGKESTNPLAFKFYDPEEIIDGKPLKDHLKFSVAFWHTFVNEGRDPFGDPTADRPWNRYTDPMDKAFA
RVDALFEFCEKLNIEYFCFHDRDIAPEGKTLRETNKILDKVVERIKERMKDSNVKLLWGTANLFSHPRYMHGAATTCSAD
VFAYAAAQVKKALEITKELGGEGYVFWGGREGYETLLNTDLGFELENLARFLRMAVDYAKRIGFTGQFLIEPKPKEPTKH
QYDFDVATAYAFLKSHGLDEYFKFNIEANHATLAGHTFQHELRMARILGKLGSIDANQGDLLLGWDTDQFPTNVYDTTLA
MYEVIKAGGFTKGGLNFDAKVRRASYKVEDLFIGHIAGMDTFALGFKVAYKLVKDGVLDKFIEEKYRSFREGIGRDIVEG
KVDFEKLEEYIIDKETIELPSGKQEYLESLINSYIVKTILELR

PROTEIN WAS CRYSTALLIZED FROM 14% JEFFAMINE ED 4000, 5 MM MGSO4, 0.5 MM COCL2, 50 MM MOPS, PH 7.0 (FOR DETAILS SEE REFERENCE 1).

xylose isolmerase from T. thermosulfurigene

DISORDERED SIDE CHAINS WERE NOT INCLUDED IN REFINEMENT.
XYLOSE ISOMERASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES

KETOLISOMERASE, XYLOSE METABOLISM, GLUCOSE-FRUCTOSE INTERCONVERSION, HYDRIDE TRANSFER, ALPHA-BETA BARREL, METALLOENZYME, THERMOPHILE

MAEFFPEIPKVQFEGKESTNPLAFKFYDPEEIIDGKPLKDHLKFSVAFWHTFVNEGRDPFGDPTADRPWNRYTDPMDKAF
ARVDALFEFCEKLNIEYFCFHDRDIAPEGKTLRETNKILDKVVERIKERMKDSNVKLLWGTANLFSHPRYMHGAATTCSA
DVFAYAAAQVKKALEITKELGGEGYVFWGGREGYETLLNTDLGFELENLARFLRMAVDYAKRIGFTGQFLIEPKPKEPTK
HQYDFDVATAYAFLKSHGLDEYFKFNIEANHATLAGHTFQHELRMARILGKLGSIDANQGDLLLGWDTDQFPTNVYDTTL
AMYEVIKAGGFTKGGLNFDAKVRRASYKVEDLFIGHIAGMDTFALGFKVAYKLVKDGVLDKFIEEKYRSFREGIGRDIVE
GKVDFEKLEEYIIDKETIELPSGKQEYLESLINSYIVKTILELR

CO BINDING SITE 2 OF MOLECULE A (HOH629 WAS ADDED AFTER LAST REFINEMENT RESULTED IN A NEW FO-FC PEAK AT THIS SITE).

CO BINDING SITE 3 OF MOLECULE A (SITE CO3 IS ON A CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AXIS: INTERPRETATION OF THE OBSERVED DENSITY PEAK AS A CO CATION WAS PRAGMATIC RATHER THAN RIGOROUS, AS THIS SITE IS CLEARLY NOT A FEATURE OF THE PROTEIN IN SOLUTION).

CO BINDING SITE 2 OF MOLECULE D (HOH629 WAS ADDED AFTER LAST REFINEMENT RESULTED IN A NEW FO-FC PEAK AT THIS SITE).

CO BINDING SITE 3 OF MOLECULE D (SITE CO3 IS ON A CRYSTALLOGRAPHIC TWO-FOLD SYMMETRY AXIS: INTERPRETATION OF THE OBSERVED DENSITY PEAK AS A CO CATION WAS PRAGMATIC RATHER THAN RIGOROUS, AS THIS SITE IS CLEARLY NOT A FEATURE OF THE PROTEIN IN SOLUTION).