HEADER PHOSPHOTRANSFERASE 25-SEP-91 1GPR COMPND GLUCOSE PERMEASE (DOMAIN IIA) (E.C.2.7.1.69) SOURCE (BACILLUS SUBTILIS) RECOMBINANT FORM AUTHOR D.-I.LIAO,O.HERZBERG REVDAT 1 31-OCT-93 1GPR 0 JRNL AUTH D.-I.LIAO,O.HERZBERG JRNL TITL REFINED CRYSTAL STRUCTURE OF IIA DOMAIN OF THE JRNL TITL 2 GLUCOSE PERMEASE OF BACILLUS SUBTILIS AT 1.9 JRNL TITL 3 ANGSTROMS RESOLUTION JRNL REF TO BE PUBLISHED JRNL REFN 353 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.-I.LIAO,G.KAPADIA,P.REDDY,M.H.SAIER JUNIOR, REMARK 1 AUTH 2 J.REIZER,O.HERZBERG REMARK 1 TITL STRUCTURE OF THE IIA DOMAIN OF THE GLUCOSE REMARK 1 TITL 2 PERMEASE OF BACILLUS SUBTILIS AT 2.2 ANGSTROMS REMARK 1 TITL 3 RESOLUTION REMARK 1 REF BIOCHEMISTRY V. 30 9583 1991 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 2 REMARK 1 AUTH G.KAPADIA,C.C.H.CHEN,P.REDDY,M.H.SAIER JUNIOR, REMARK 1 AUTH 2 J.REIZER,O.HERZBERG REMARK 1 TITL CRYSTALLIZATION OF THE IIA DOMAIN OF THE GLUCOSE REMARK 1 TITL 2 PERMEASE OF BACILLUS SUBTILIS REMARK 1 REF J.MOL.BIOL. V. 221 1079 1991 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 3 REMARK 1 AUTH D.WORTHYLAKE,N.D.MEADOW,S.ROSEMAN,D.-I.LIAO, REMARK 1 AUTH 2 O.HERZBERG,S.J.REMINGTON REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE ESCHERICHIA REMARK 1 TITL 2 COLI PHOSPHOCARRIER PROTEIN III==GLC== REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 88 10382 1991 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 REMARK 2 REMARK 2 RESOLUTION. 1.9 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM TNT REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS REMARK 3 R VALUE 0.156 REMARK 3 RMSD BOND DISTANCES 0.021 ANGSTROMS REMARK 3 RMSD BOND ANGLES 3.4 DEGREES REMARK 4 REMARK 4 THE PHOSPHOENOLPYRUVATE: GLYCOSE PHOSPHOTRANSFERASE SYSTEM REMARK 4 (PTS) IS A BACTERIAL SUGAR TRANSPORT SYSTEM IN WHICH THE REMARK 4 TRANSPORT IS LINKED TO A CHAIN OF FIVE PHOSPHORYLATION REMARK 4 STEPS: PEP TO ENZYME I, ENZYME I TO HPR, HPR TO IIA, IIA REMARK 4 TO IIB, IIB TO THE SUGAR. THE PHOSPHORYLATION OF THE IIA REMARK 4 DOMAIN OCCURS ON THE INVARIANT HIS 83. AN ADJACENT REMARK 4 INVARIANT HISTIDINE (HIS 68) IS ALSO FUNCTIONALLY REMARK 4 IMPORTANT. REMARK 5 REMARK 5 THE BACILLUS SUBTILIS GLUCOSE PERMEASE (ENZYME II) REMARK 5 CONSISTS OF THREE DOMAINS IIA, IIB, AND IIC, RESIDING ON A REMARK 5 SINGLE POLYPEPTIDE CHAIN, WITH THE ORDER IICBA. THE REMARK 5 RECOMBINANT IIA DOMAIN (162 AMINO ACID RESIDUES) IS A REMARK 5 SOLUBLE PROTEIN. SEQUENTIAL NUMBERING OF THIS RECOMBINANT REMARK 5 PROTEIN IS USED HERE. REMARK 6 REMARK 6 THE MODEL INCLUDES ALL BUT THE FIRST THREE N-TERMINAL AND REMARK 6 ONE C-TERMINAL AMINO ACID RESIDUES WHICH ARE DISORDERED. REMARK 7 REMARK 7 THERE ARE ELEVEN PROLINE RESIDUES ALL OF WHICH ARE IN THE REMARK 7 TRANS CONFORMATION. REMARK 8 REMARK 8 SECONDARY STRUCTURE ASSIGNMENT IS ACCORDING TO KABSCH AND REMARK 8 SANDER (BIOPOLYMERS 22, 2577-2637, 1983) EXCEPT RESIDUES REMARK 8 GLU 12 - SER 17 CLEARLY ADOPT A BETA STRAND CONFORMATION, REMARK 8 BUT ARE NOT INVOLVED IN HYDROGEN BONDING WITH OTHER REMARK 8 STRANDS, AND THUS ARE NOT IDENTIFIED BY THE DSSP PROGRAM. REMARK 8 BRIDGES OF SINGLE RESIDUES ARE NOT INCLUDED IN THE REMARK 8 ASSIGNMENT. SEQRES 1 162 MET ILE ALA GLU PRO LEU GLN ASN GLU ILE GLY GLU GLU SEQRES 2 162 VAL PHE VAL SER PRO ILE THR GLY GLU ILE HIS PRO ILE SEQRES 3 162 THR ASP VAL PRO ASP GLN VAL PHE SER GLY LYS MET MET SEQRES 4 162 GLY ASP GLY PHE ALA ILE LEU PRO SER GLU GLY ILE VAL SEQRES 5 162 VAL SER PRO VAL ARG GLY LYS ILE LEU ASN VAL PHE PRO SEQRES 6 162 THR LYS HIS ALA ILE GLY LEU GLN SER ASP GLY GLY ARG SEQRES 7 162 GLU ILE LEU ILE HIS PHE GLY ILE ASP THR VAL SER LEU SEQRES 8 162 LYS GLY GLU GLY PHE THR SER PHE VAL SER GLU GLY ASP SEQRES 9 162 ARG VAL GLU PRO GLY GLN LYS LEU LEU GLU VAL ASP LEU SEQRES 10 162 ASP ALA VAL LYS PRO ASN VAL PRO SER LEU MET THR PRO SEQRES 11 162 ILE VAL PHE THR ASN LEU ALA GLU GLY GLU THR VAL SER SEQRES 12 162 ILE LYS ALA SER GLY SER VAL ASN ARG GLU GLN GLU ASP SEQRES 13 162 ILE VAL LYS ILE GLU LYS FORMUL 2 HOH *100(H2 O1) HELIX 1 H1 ILE 26 ASP 28 5 HELIX 2 H2 GLN 32 SER 35 1 HELIX 3 H3 VAL 89 LEU 91 5 HELIX 4 H4 LEU 117 VAL 120 1 HELIX 5 H5 LYS 121 ASN 123 5 SHEET 1 S1 8 SER 149 VAL 150 0 SHEET 2 S1 8 GLY 21 PRO 25 -1 SHEET 3 S1 8 ASP 41 PRO 47 -1 SHEET 4 S1 8 THR 129 PHE 133 -1 SHEET 5 S1 8 GLU 79 HIS 83 -1 SHEET 6 S1 8 ALA 69 SER 74 -1 SHEET 7 S1 8 GLY 58 VAL 63 -1 SHEET 8 S1 8 ARG 105 VAL 106 -1 SHEET 1 S2 3 ILE 51 VAL 53 0 SHEET 2 S2 3 LYS 111 VAL 115 -1 SHEET 3 S2 3 PHE 96 SER 98 -1 SHEET 1 S3 2 SER 143 ILE 144 0 SHEET 2 S3 2 VAL 158 LYS 159 -1 CRYST1 74.220 54.940 66.960 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.013473 0.000000 0.000000 0.00000 SCALE2 0.000000 0.018202 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014934 0.00000